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Conserved domains on  [gi|578809600|ref|XP_006714469|]
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cyclin-dependent kinase-like 2 isoform X3 [Homo sapiens]

Protein Classification

cyclin-dependent kinase-like( domain architecture ID 10167599)

cyclin-dependent kinase-like (CDKL) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and is regulated by its cognate cyclin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
2-287 0e+00

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


:

Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 607.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd07846   81 FVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLP 241
Cdd:cd07846  161 VATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQKNPLFAGVRLP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 242 EIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07846  241 EVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
 
Name Accession Description Interval E-value
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
2-287 0e+00

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 607.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd07846   81 FVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLP 241
Cdd:cd07846  161 VATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQKNPLFAGVRLP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 242 EIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07846  241 EVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-287 7.00e-97

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 294.05  E-value: 7.00e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600     4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERI-LREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    84 DHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaAPGEVYTDYVA 163
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL-DPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   164 TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfnknpvfagvrlpei 243
Cdd:smart00220 159 TPEYMAPEVLLGK-GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIG--------------------------- 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 578809600   244 KEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:smart00220 211 KPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-288 1.05e-75

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 240.88  E-value: 1.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFARTLAAPGEVY 158
Cdd:PLN00009  81 EYLDLDLKKHMDSSPDfAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGLARAFGIPVRTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQelfnknpVFAGV 238
Cdd:PLN00009 161 THEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGT--PNEE-------TWPGV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 239 -RLPEIKEREP------LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:PLN00009 232 tSLPDYKSAFPkwppkdLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
Pkinase pfam00069
Protein kinase domain;
4-287 1.12e-60

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 199.01  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   84 DHTILDDLELFPNGLDYQVVQKYLFQIINGIgfchshniihrdikpenilvsqsgvvklcdfgfartlaAPGEVYTDYVA 163
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL--------------------------------------ESGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  164 TRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClgnliPRHQELFNKNpvfagvrlpei 243
Cdd:pfam00069 123 TPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQ-----PYAFPELPSN----------- 185
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578809600  244 kereplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:pfam00069 186 ------------LSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
3-286 3.65e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 179.05  E-value: 3.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLE--SDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:COG0515    8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPelAADPEARERF-RREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLeLFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:COG0515   87 EYVEGESLADL-LRRRGpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVA-TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfnknpvfagv 238
Cdd:COG0515  166 GTVVgTPGYMAPEQARGE-PVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLR---------------------- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 239 rlpeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:COG0515  223 -----EPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAAAL 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
4-206 1.01e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 107.96  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGsyGMVMKCRNKDT--GRIVAIKkFLESD---DDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:NF033483   9 YEIGERIGRG--GMAEVYLAKDTrlDRDVAVK-VLRPDlarDPEFVARFR-REAQSAASLSHPNIVSVYDVGEDGGIPYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDL--ELFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:NF033483  85 VMEYVDGRTLKDYirEHGP--LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTM 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 157 VYTDYV-ATRWYRAPELlvgdVKYGKA---VDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:NF033483 163 TQTNSVlGTVHYLSPEQ----ARGGTVdarSDIYSLGIVLYEMLTGRPPFDGDS 212
 
Name Accession Description Interval E-value
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
2-287 0e+00

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 607.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07846    1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd07846   81 FVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLP 241
Cdd:cd07846  161 VATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELFQKNPLFAGVRLP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 242 EIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07846  241 EVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
2-287 0e+00

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 553.46  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV-YTD 160
Cdd:cd07833   81 YVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASpLTD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRL 240
Cdd:cd07833  161 YVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPPSHQELFSSNPRFAGVAF 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 241 PEIKEREPLERRYP-KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07833  241 PEPSQPESLERRYPgKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
2-287 3.02e-165

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 469.55  E-value: 3.02e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07847    1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd07847   81 YCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLP 241
Cdd:cd07847  161 VATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQIFSTNQFFKGLSIP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 242 EIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07847  241 EPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
4-287 2.09e-106

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 319.43  E-value: 2.09e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIrLDNEEEG-IPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYV 162
Cdd:cd07829   80 CDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGIPLRTYTHEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----NLIPRHQELFNKNPVFagv 238
Cdd:cd07829  160 VTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGtpteESWPGVTKLPDYKPTF--- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 239 rlpEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07829  237 ---PKWPKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
3-287 3.27e-103

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 311.54  E-value: 3.27e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd07848    2 KFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV-YTDY 161
Cdd:cd07848   82 VEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNAnYTEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLP 241
Cdd:cd07848  162 VATRWYRSPELLLG-APYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFYSNPRFHGLRFP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 242 EIKEREPLERRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07848  241 AVNHPQSLERRYLGiLSGVLLDLMKNLLKLNPTDRYLTEQCLNHPAF 287
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
4-287 7.00e-97

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 294.05  E-value: 7.00e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600     4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERI-LREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    84 DHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaAPGEVYTDYVA 163
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQL-DPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   164 TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfnknpvfagvrlpei 243
Cdd:smart00220 159 TPEYMAPEVLLGK-GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIG--------------------------- 210
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 578809600   244 KEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:smart00220 211 KPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
4-287 3.87e-95

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 290.73  E-value: 3.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIrLETEDEG-VPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd07835   80 LDLDLKKYMDSSPLtGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVPVRTYTHE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPrhqelfnKNPVFAGVR-L 240
Cdd:cd07835  160 VVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGT--P-------DEDVWPGVTsL 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 241 PEIK------EREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07835  231 PDYKptfpkwARQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
4-287 4.33e-92

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 282.89  E-value: 4.33e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF---LESDDDKMvkkiAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLV 79
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMkkkFYSWEECM----NLREVKSLRKLnEHPNIVKLKEVFRENDELYFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILD-----DLELFPNGldyqVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaap 154
Cdd:cd07830   77 FEYMEGNLYQlmkdrKGKPFSES----VIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAR----- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 gEV-----YTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLI----PRH 225
Cdd:cd07830  148 -EIrsrppYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTkqdwPEG 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 226 QELFNKnpvfAGVRLPEIKErEPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07830  227 YKLASK----LGFRFPQFAP-TSLHQLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-287 2.54e-90

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 277.19  E-value: 2.54e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLEsddDKMVKKIAMREIKLLKQLR----HENLVNLLEVC--KKKKRWY 77
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKN---DFRHPKAALREIKLLKHLNdvegHPNIVKLLDVFehRGGNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFARTLAAPge 156
Cdd:cd05118   78 LVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFTSP-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliprhqelfnknpvfa 236
Cdd:cd05118  156 PYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGT---------------- 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 237 gvrlpeikereplerrypklsEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd05118  220 ---------------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
3-287 5.60e-85

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 265.20  E-value: 5.60e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF---LESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIklgERKEAKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDhtilDDLE-LFPNG-LDYQV--VQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPG 155
Cdd:cd07841   81 FEFME----TDLEkVIKDKsIVLTPadIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSFGSPN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQElfnkNPVF 235
Cdd:cd07841  157 RKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGT--PTEEN----WPGV 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 236 AgvRLP---EIKERE--PLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07841  231 T--SLPdyvEFKPFPptPLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYF 285
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
4-287 1.25e-84

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 264.04  E-value: 1.25e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV------CKKKKRWY 77
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIvtskgsAKYKGSIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHtildDLelfpNGLDYQVVQK--------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd07840   81 MVFEYMDH----DL----TGLLDNPEVKftesqikcYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAPGEV-YTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQEL 228
Cdd:cd07840  153 PYTKENNAdYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPG 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 229 FNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07840  233 VSDLPWFENLKPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
3-287 2.95e-84

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 262.65  E-value: 2.95e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLR-HENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE-VYTD 160
Cdd:cd07832   81 YMLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDPrLYSH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----NLIPRHQELfnknPVFA 236
Cdd:cd07832  161 QVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGtpneKTWPELTSL----PDYN 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 237 GVRLPEIKeREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07832  237 KITFPESK-GIRLEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
4-287 1.11e-83

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 261.28  E-value: 1.11e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHtildDLELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd07860   82 HQ----DLKKFmdasaLTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQelfnknpVFAGV 238
Cdd:cd07860  158 THEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGT--PDEV-------VWPGV 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 239 -RLPEIK------EREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07860  229 tSMPDYKpsfpkwARQDFSKVVPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
3-288 2.62e-83

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 261.69  E-value: 2.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW-----Y 77
Cdd:cd07834    1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPEefndvY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVD---HTILDDlelfPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd07834   81 IVTELMEtdlHKVIKS----PQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVY--TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnlIPRHQEL-FNK 231
Cdd:cd07834  157 EDKGflTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLG--TPSEEDLkFIS 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 232 NPVFAG--VRLPEiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07834  235 SEKARNylKSLPK-KPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLA 292
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
3-287 1.55e-80

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 253.11  E-value: 1.55e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIrLESEEEG-VPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd07861   80 FLSMDLKKYLDSLPKGkyMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGIPVRVYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliprhqelfNKNPVFAGV- 238
Cdd:cd07861  160 HEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGT---------PTEDIWPGVt 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 239 RLPEIKEREP------LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07861  231 SLPDYKNTFPkwkkgsLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
2-288 3.21e-79

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 251.71  E-value: 3.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKK----FLESDDdkmvkkiA---MREIKLLKQLR-HENLVNLLEVCKKK 73
Cdd:cd07852    7 RRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKifdaFRNATD-------AqrtFREIMFLQELNdHPNIIKLLNVIRAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 --KRWYLVFEFVD--------HTILDDlelfpngldyqVVQKY-LFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKL 142
Cdd:cd07852   80 ndKDIYLVFEYMEtdlhavirANILED-----------IHKQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 143 CDFGFARTLAAPGE-----VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC 217
Cdd:cd07852  149 ADFGLARSLSQLEEddenpVLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEV 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 218 LGNliPRHQELFNKNPVFAGV---RLPeIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07852  229 IGR--PSAEDIESIQSPFAATmleSLP-PSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVA 299
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
3-287 6.26e-78

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 246.65  E-value: 6.26e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLEsddDKMVKKiamREIKLLKQLRHENLVNLL----EVCKKKKRWYL 78
Cdd:cd14137    5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQ---DKRYKN---RELQIMRRLKHPNIVKLKyffySSGEKKDEVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 --VFEFVDHTILDDLELFP---NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ-SGVVKLCDFGFARTLA 152
Cdd:cd14137   79 nlVMEYMPETLYRVIRHYSknkQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPeTGVLKLCDFGSAKRLV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 aPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQELFNKN 232
Cdd:cd14137  159 -PGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGT--PTREQIKAMN 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 233 PVFAGVRLPEIKeREPLERRYPKLSE-VVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14137  236 PNYTEFKFPQIK-PHPWEKVFPKRTPpDAIDLLSKILVYNPSKRLTALEALAHPFF 290
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
3-287 2.74e-76

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 243.05  E-value: 2.74e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKR------- 75
Cdd:cd07865   13 KYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKATpynrykg 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 -WYLVFEFVDHtildDLELFPNG----LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd07865   93 sIYLVFEFCEH----DLAGLLSNknvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAP----GEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQ 226
Cdd:cd07865  169 FSLAknsqPNRYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVW 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 227 ELFNKNPVFAGVRLPEIKEREPLERRYPKLSEV-VIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07865  249 PGVDKLELFKKMELPQGQKRKVKERLKPYVKDPyALDLIDKLLVLDPAKRIDADTALNHDFF 310
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1-288 1.05e-75

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 240.88  E-value: 1.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFARTLAAPGEVY 158
Cdd:PLN00009  81 EYLDLDLKKHMDSSPDfAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGLARAFGIPVRTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQelfnknpVFAGV 238
Cdd:PLN00009 161 THEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGT--PNEE-------TWPGV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 239 -RLPEIKEREP------LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:PLN00009 232 tSLPDYKSAFPkwppkdLATVVPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
2-287 6.55e-75

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 238.66  E-value: 6.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdddKMVKKI------AMREIKLLKQLRHENLVNLLEVC--KKK 73
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKL------KMEKEKegfpitSLREINILLKLQHPNIVTVKEVVvgSNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd07843   79 DKIYMVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNP 233
Cdd:cd07843  159 PLKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKIWPGFSELP 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 234 vFAGVRLPEIKEREPLERRYP--KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07843  239 -GAKKKTFTKYPYNQLRKKFPalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
4-287 1.07e-73

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 235.63  E-value: 1.07e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLR---HENLVNLLEVCKKKKRW---- 76
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRTDrelk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 -YLVFEFVDHtildDLELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARt 150
Cdd:cd07838   81 lTLVFEHVDQ----DLATYldkcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLAR- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 laapgeVYTDY------VATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnlIPR 224
Cdd:cd07838  156 ------IYSFEmaltsvVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIG--LPS 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 225 HQElFNKNPVFAGVRLPEiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07838  227 EEE-WPRNSALPRSSFPS-YTPRPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
4-287 9.38e-73

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 233.75  E-value: 9.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVC--------KKKKR 75
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAverpdkskRKRGS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR------ 149
Cdd:cd07866   90 VYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARpydgpp 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 -TLAAPGEV----YTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNL--- 221
Cdd:cd07866  170 pNPKGGGGGgtrkYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPtee 249
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 222 -IPRHQELFNKNPVFAGVRLPEIkerepLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07866  250 tWPGWRSLPGCEGVHSFTNYPRT-----LEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
4-287 1.13e-71

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 230.35  E-value: 1.13e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIrLEHEEG--APFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYV 162
Cdd:cd07844   80 LDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSVPSKTYSNEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDI-DQLYHIMMCLGNLIPRHQELFNKNPVFAGVRLP 241
Cdd:cd07844  160 VTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTPTEETWPGVSSNPEFKPYSFP 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 242 EIKeREPLERRYPKLSEVV--IDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07844  240 FYP-PRPLINHAPRLDRIPhgEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
4-288 1.85e-70

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 228.02  E-value: 1.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKiAMREIKLLKQLRHENLVNLLEVC--KKKKRWYLVF 80
Cdd:cd07845    9 FEKLNRIGEGTYGIVYRARDTTSGEIVALKKVrMDNERDGIPIS-SLREITLLLNLRHPNIVELKEVVvgKHLDSIFLVM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd07845   88 EYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPAKPMTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRL 240
Cdd:cd07845  168 KVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIWPGFSDLPLVGKFTL 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 241 PEikerEP---LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07845  248 PK----QPynnLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
3-287 1.12e-69

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 225.00  E-value: 1.12e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd07839    1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHtildDLELF---PNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd07839   81 CDQ----DLKKYfdsCNGdIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGIPVRCY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYHIMMCLGNliPRHQElfnknpvFAG 237
Cdd:cd07839  157 SAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGT--PTEES-------WPG 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 238 V-RLPEIKEREP------LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07839  228 VsKLPDYKPYPMypattsLVNVVPKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
4-287 7.50e-69

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The Pho85 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 222.74  E-value: 7.50e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKE-IHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHtildDLELF------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV 157
Cdd:cd07836   81 DK----DLKKYmdthgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----NLIPRHQELFNKNP 233
Cdd:cd07836  157 FSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGtpteSTWPGISQLPEYKP 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 234 VFagvrlpEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07836  237 TF------PRYPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
3-289 7.16e-68

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 221.86  E-value: 7.16e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKR-----WY 77
Cdd:cd07858    6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHReafndVY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVD---HTILDDlelfPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd07858   86 IVYELMDtdlHQIIRS----SQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQEL-FNKNP 233
Cdd:cd07858  162 GDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGS--PSEEDLgFIRNE 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 234 -VFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd07858  240 kARRYIRSLPYTPRQSFARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLAS 296
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2-287 1.03e-67

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 220.09  E-value: 1.03e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmVKKIAMREIKLLKQLRHEN-LVNLLEV----CKKKKR 75
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTrLEMEEEG-VPSTALREVSLLQMLSQSIyIVRLLDVehveENGKPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDhtilDDLELF--------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFG 146
Cdd:cd07837   80 LYLVFEYLD----TDLKKFidsygrgpHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQ 226
Cdd:cd07837  156 LGRAFTIPIKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGT--PNEE 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 227 elfnknpVFAGVR-------LPEIKEREpLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07837  234 -------VWPGVSklrdwheYPQWKPQD-LSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYF 293
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
2-288 7.92e-67

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 219.10  E-value: 7.92e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKK-----KRW 76
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKK-ISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPtfesfKDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDhTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtLAAPGE 156
Cdd:cd07849   84 YIVQELME-TDLYKL-IKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR-IADPEH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VY----TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQELFN-K 231
Cdd:cd07849  161 DHtgflTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGT--PSQEDLNCiI 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 232 NP-VFAGVR-LPeIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07849  239 SLkARNYIKsLP-FKPKVPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLE 296
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
9-287 1.79e-66

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 215.46  E-value: 1.79e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-T 86
Cdd:cd06606    7 LLGKGSFGSVYLALNLDTGELMAVKEVeLSGDSEEELEAL-EREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGgS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA--APGEVYTDYVAT 164
Cdd:cd06606   86 LASLLKKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAeiATGEGTKSLRGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIDQLYHIMMCLGnliprhqelFNKNPvfagvrlPEIK 244
Cdd:cd06606  165 PYWMAPEVIRGE-GYGRAADIWSLGCTVIEMATGKPPW---SELGNPVAALFKIG---------SSGEP-------PPIP 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578809600 245 EReplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06606  225 EH---------LSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1-286 5.02e-65

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 213.51  E-value: 5.02e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVC---------- 70
Cdd:cd07864    6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVtdkqdaldfk 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  71 KKKKRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd07864   86 KDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLARL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAA-PGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELF 229
Cdd:cd07864  166 YNSeESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPAVWPDV 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 230 NKNPVFAGVRlPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd07864  246 IKLPYFNTMK-PKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
3-287 1.27e-62

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 207.52  E-value: 1.27e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKD--TGRIVAIKKFlESDDDKM--VKKIAMREIKLLKQLRHENLVNLLEVC--KKKKRW 76
Cdd:cd07842    1 KYEIEGCIGRGTYGRVYKAKRKNgkDGKEYAIKKF-KGDKEQYtgISQSACREIALLRELKHENVVSLVEVFleHADKSV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILD--------DLELFPNGldyqVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV----SQSGVVKLCD 144
Cdd:cd07842   80 YLLFDYAEHDLWQiikfhrqaKRVSIPPS----MVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 145 FGFARTLAAPGEVYTD---YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSD---------IDQLY 212
Cdd:cd07842  156 LGLARLFNAPLKPLADldpVVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRDQLE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 213 HIMMCLGNLIPRHQELFNKNPVFAGVRLPEIKEREP---LERRY---PKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd07842  236 RIFEVLGTPTEKDWPDIKKMPEYDTLKSDTKASTYPnslLAKWMhkhKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPY 315

                 .
gi 578809600 287 F 287
Cdd:cd07842  316 F 316
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
2-287 1.28e-62

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 208.30  E-value: 1.28e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV------CKKKKR 75
Cdd:cd07851   15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVftpassLEDFQD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVD---HTILDDLELfpnglDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd07851   95 VYLVTHLMGadlNNIVKCQKL-----SDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 apgEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRhQELFNK- 231
Cdd:cd07851  170 ---DEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGT--PD-EELLKKi 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 232 --NPVFAGVR-LPEIKeREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07851  244 ssESARNYIQsLPQMP-KKDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1-291 4.94e-62

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 205.62  E-value: 4.94e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd07873    1 LETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIrLEHEEGAPCT--AIREVSLLKDLKHANIVTLHDIIHTEKSLTLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd07873   79 FEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVR 239
Cdd:cd07873  159 NEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKSYN 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 240 LPEIKErEPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDG 291
Cdd:cd07873  239 YPKYRA-DALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLG 289
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1-287 1.23e-61

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 204.09  E-value: 1.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd07871    4 LETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIrLEHEEGAPCT--AIREVSLLKNLKHANIVTLHDIIHTERCLTLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd07871   82 FEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVR 239
Cdd:cd07871  162 NEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSNEEFRSYL 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 240 LPEIKErEPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07871  242 FPQYRA-QPLINHAPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
Pkinase pfam00069
Protein kinase domain;
4-287 1.12e-60

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 199.01  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   84 DHTILDDLELFPNGLDYQVVQKYLFQIINGIgfchshniihrdikpenilvsqsgvvklcdfgfartlaAPGEVYTDYVA 163
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL--------------------------------------ESGSSLTTFVG 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  164 TRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClgnliPRHQELFNKNpvfagvrlpei 243
Cdd:pfam00069 123 TPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQ-----PYAFPELPSN----------- 185
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 578809600  244 kereplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:pfam00069 186 ------------LSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
4-287 1.22e-60

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 201.35  E-value: 1.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvKKIAMREIKLLKQLR-HENLVNLLEVC--KKKKRWYLVF 80
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLE-QVNNLREIQALRRLSpHPNILRLIEVLfdRKTGRLALVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQsGVVKLCDFGFARTLAAPGEvYTD 160
Cdd:cd07831   80 ELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGSCRGIYSKPP-YTE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNK----NPVFA 236
Cdd:cd07831  158 YISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVLKKFRKsrhmNYNFP 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 237 GvrlpeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07831  238 S------KKGTGLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
2-286 5.10e-60

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 201.26  E-value: 5.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV-CKKKKRWYLVF 80
Cdd:cd07856   10 TRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLEDIYFVT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVD---HTILDDlelfpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgev 157
Cdd:cd07856   90 ELLGtdlHRLLTS-----RPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQ--- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNlIPRH--QELFNKNPVF 235
Cdd:cd07856  162 MTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGT-PPDDviNTICSENTLR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 236 AGVRLPEiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd07856  241 FVQSLPK-RERVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPY 290
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
2-288 1.52e-59

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 200.28  E-value: 1.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW----- 76
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYadfkd 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 -YLVFEFVD---HTILDDLElfPNGLDYqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd07855   85 vYVVLDLMEsdlHHIIHSDQ--PLTLEH--IRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVY----TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQEL 228
Cdd:cd07855  161 TSPEEHkyfmTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGT--PSQAVI 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 229 fnkNPVFAG-VR-----LPEiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07855  239 ---NAIGADrVRryiqnLPN-KQPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLA 300
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
11-195 1.83e-58

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 193.26  E-value: 1.83e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TILD 89
Cdd:cd00180    2 GKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLLEEL-LREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGgSLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATR-WYR 168
Cdd:cd00180   81 LLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTGGTTpPYY 160
                        170       180
                 ....*....|....*....|....*..
gi 578809600 169 APELLVGDVKYGKAVDVWAIGCLVTEM 195
Cdd:cd00180  161 APPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1-291 1.52e-57

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 194.05  E-value: 1.52e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd07872    5 METYIKLEKLGEGTYATVFKGRSKLTENLVALKE-IRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd07872   84 EYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPVFAGVRL 240
Cdd:cd07872  164 EVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISSNDEFKNYNF 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 241 PEIKErEPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDG 291
Cdd:cd07872  244 PKYKP-QPLINHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSLG 293
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
4-289 1.72e-57

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 194.55  E-value: 1.72e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDT--GRIVAIKKFLESDDDKMVKKIAMREIKLLKQLR-HENLVNLLEVckkkkrwylvf 80
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITNVFSKKILAKRALRELKLLRHFRgHKNITCLYDM----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDY---QVV-----------QKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd07857   71 DIVFPGNFNELYLYEELMEAdlhQIIrsgqpltdahfQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTLAA-PGEV---YTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNli 222
Cdd:cd07857  151 LARGFSEnPGENagfMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGT-- 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 223 PRHQEL--FNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd07857  229 PDEETLsrIGSPKAQNYIRSLPNIPKKPFESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAI 297
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
2-287 2.80e-57

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 192.94  E-value: 2.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRN-KDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLR---HENLVNLLEVCK-----K 72
Cdd:cd07862    1 QQYECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTvsrtdR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  73 KKRWYLVFEFVDHTILDDLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL 151
Cdd:cd07862   81 ETKLTLVFEHVDQDLTTYLDKVPEpGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPGEVyTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnlIPRHQELFNK 231
Cdd:cd07862  161 SFQMAL-TSVVVTLWYRAPEVLL-QSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIG--LPGEEDWPRD 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 232 npvfagVRLPE----IKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07862  237 ------VALPRqafhSKSAQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYF 290
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
4-287 3.00e-55

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 187.48  E-value: 3.00e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd07870    2 YLNLEKLGEGSYATVYKGISRINGQLVALK-VISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVA 163
Cdd:cd07870   81 HTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDI-DQLYHIMMCLG----NLIPRHQELFNKNP-VFAG 237
Cdd:cd07870  161 TLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLGvpteDTWPGVSKLPNYKPeWFLP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 238 VRLPEIKEREPLERRYPKLSevviDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07870  241 CKPQQLRVVWKRLSRPPKAE----DLASQMLMMFPKDRISAQDALLHPYF 286
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
3-287 3.01e-55

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 187.48  E-value: 3.01e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLR---HENLVNLLEVC-----KKKK 74
Cdd:cd07863    1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCatsrtDRET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVDHTILDDLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd07863   81 KVTLVFEHVDQDLRTYLDKVPPpGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYSC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVyTDYVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnlIPRHQELfnknP 233
Cdd:cd07863  161 QMAL-TPVVVTLWYRAPEVLLQST-YATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIG--LPPEDDW----P 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 234 VfaGVRLPE----IKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07863  233 R--DVTLPRgafsPRGPRPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
2-290 1.13e-54

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 187.28  E-value: 1.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLG-LVGEGSYGMVMKCRNKDTGRIVAIKKF----LESDDDKMVKKIAM--------REIKLLKQLRHENLVNLLE 68
Cdd:PTZ00024   8 ERYIQKGaHLGEGTYGKVEKAYDTLTGKIVAIKKVkiieISNDVTKDRQLVGMcgihfttlRELKIMNEIKHENIMGLVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 VCKKKKRWYLVFEFVDHtildDL-ELFPNGLDYQVVQK--YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:PTZ00024  88 VYVEGDFINLVMDIMAS----DLkKVVDRKIRLTESQVkcILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARTLA--------------APGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQL 211
Cdd:PTZ00024 164 GLARRYGyppysdtlskdetmQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 212 YHIMMCLGNLIPRHQELFNKNPVFAgvrlpEIKEREP--LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:PTZ00024 244 GRIFELLGTPNEDNWPQAKKLPLYT-----EFTPRKPkdLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKS 318

                 .
gi 578809600 290 D 290
Cdd:PTZ00024 319 D 319
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
3-288 1.30e-54

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 187.30  E-value: 1.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVC-----KKKKRWY 77
Cdd:cd07859    1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMlppsrREFKDIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVD---HTIL---DDLelfpNGLDYQVvqkYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-- 149
Cdd:cd07859   81 VVFELMEsdlHQVIkanDDL----TPEHHQF---FLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARva 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAPGEVY-TDYVATRWYRAPElLVGDV--KYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPRHQ 226
Cdd:cd07859  154 FNDTPTAIFwTDYVATRWYRAPE-LCGSFfsKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETI 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 227 ELFNKNPVFAGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07859  233 SRVRNEKARRYLSSMRKKQPVPFSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFK 294
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
3-284 1.33e-54

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 184.60  E-value: 1.33e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKkiamREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidkKKLKSEDEEMLR----REIEILKRLDHPNIVKLYEVFEDDKNLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDhtildDLELFP-----NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFART 150
Cdd:cd05117   77 VMELCT-----GGELFDrivkkGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAaPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhQELFN 230
Cdd:cd05117  152 FE-EGEKLKTVCGTPYYVAPEVLKGK-GYGKKCDIWSLGVILYILLCGYPPFYGETE------------------QELFE 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 231 KnpvfagvrlpeIKEREPL--ERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd05117  212 K-----------ILKGKYSfdSPEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNH 256
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
3-284 1.69e-54

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 183.87  E-value: 1.69e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKkiamREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKiidkSKLKEEIEEKIK----REIEIMKLLNHPNIIKLYEVIETENKIYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTilddlELF----PNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtLAA 153
Cdd:cd14003   77 VMEYASGG-----ELFdyivNNGrLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSN-EFR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhQELFNKnp 233
Cdd:cd14003  151 GGSLLKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDND------------------SKLFRK-- 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 234 vfagvrlpeIKEREPleRRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14003  211 ---------ILKGKY--PIPSHLSPDARDLIRRMLVVDPSKRITIEEILNH 250
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
2-301 2.35e-54

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 186.78  E-value: 2.35e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV---CKKKKRWYL 78
Cdd:cd07877   17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVftpARSLEEFND 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFeFVDHTILDDLE--LFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapgE 156
Cdd:cd07877   97 VY-LVTHLMGADLNniVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTD---D 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPrhqELFNKNPVFA 236
Cdd:cd07877  173 EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGA---ELLKKISSES 249
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 237 G----VRLPEIKEREpLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM------DGFAERFSQELQ 301
Cdd:cd07877  250 ArnyiQSLTQMPKMN-FANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQyhdpddEPVADPYDQSFE 323
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
2-288 3.72e-54

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 186.31  E-value: 3.72e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV------CKKKKR 75
Cdd:cd07880   15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVftpdlsLDRFHD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDhTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlaAPG 155
Cdd:cd07880   95 FYLVMPFMG-TDLGKL-MKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ--TDS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVyTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----NLIPRHQELFNK 231
Cdd:cd07880  171 EM-TGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGtpskEFVQKLQSEDAK 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 232 NPVfagVRLPEIKEREpLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07880  250 NYV---KKLPRFRKKD-FRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFE 302
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2-287 5.03e-54

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 184.51  E-value: 5.03e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALK-VIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd07869   84 YVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDI-DQLYHIMMCLGNLIPRHQELFNKNPVFAGVRL 240
Cdd:cd07869  164 VVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIqDQLERIFLVLGTPNEDTWPGVHSLPHFKPERF 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 241 pEIKEREPLERRYPKLSEV--VIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07869  244 -TLYSPKNLRQAWNKLSYVnhAEDLASKLLQCFPKNRLSAQAALSHEYF 291
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
3-276 1.65e-53

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 181.63  E-value: 1.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLE--SDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPelAEDEEFRERF-LREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDL--ELFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd14014   80 EYVEGGSLADLlrERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVA-TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnliprhqelfnknpvfag 237
Cdd:cd14014  158 TGSVLgTPAYMAPEQARGG-PVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHL---------------------- 214
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 578809600 238 vrlpeIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd14014  215 -----QEAPPPPSPLNPDVPPALDAIILRALAKDPEERP 248
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
4-287 2.67e-53

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 182.74  E-value: 2.67e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIK--KflesdDDKMVKKIAMREIKLLKQLRH------ENLVNLLE------- 68
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKiiR-----NKKRFHQQALVEVKILKHLNDndpddkHNIVRYKDsfifrgh 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 VCkkkkrwyLVFEFVDHTILDDLEL--FpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG--VVKLCD 144
Cdd:cd14210   90 LC-------IVFELLSINLYELLKSnnF-QGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSksSIKVID 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 145 FG---FArtlaapGE-VYTdYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG- 219
Cdd:cd14210  162 FGsscFE------GEkVYT-YIQSRFYRAPEVILG-LPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGv 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 220 ---NLI---PRHQELF----NKNPVFAGVRlpeiKEREP----LERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd14210  234 ppkSLIdkaSRRKKFFdsngKPRPTTNSKG----KKRRPgsksLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHP 309

                 ..
gi 578809600 286 FF 287
Cdd:cd14210  310 WI 311
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
11-287 8.19e-53

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 180.06  E-value: 8.19e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKF--------LESDDDKMVKKIAM----REIKLLKQLRHENLVNLLEVCK--KKKRW 76
Cdd:cd14008    2 GRGSFGKVKLALDTETGQLYAIKIFnksrlrkrREGKNDRGKIKNALddvrREIAIMKKLDHPNIVRLYEVIDdpESDKL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDH--TILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd14008   82 YLVLEYCEGgpVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFEDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDVKY--GKAVDVWAIG-CLVTeMFMGEPLFPGDSdIDQLYHimmclgnliprhqelfnk 231
Cdd:cd14008  162 NDTLQKTAGTPAFLAPELCDGDSKTysGKAADIWALGvTLYC-LVFGRLPFNGDN-ILELYE------------------ 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 232 npvfagvrlpEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14008  222 ----------AIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
2-288 1.05e-52

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 182.41  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKK------KR 75
Cdd:cd07879   15 ERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAvsgdefQD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDhtiLDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlaAPG 155
Cdd:cd07879   95 FYLVMPYMQ---TDLQKIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARH--ADA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVyTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----NLIPRHQELFNK 231
Cdd:cd07879  170 EM-TGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGvpgpEFVQKLEDKAAK 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 232 NPVFAGVRLPeikeREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07879  249 SYIKSLPKYP----RKDFSTLFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFD 301
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
2-286 2.42e-52

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 178.60  E-value: 2.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDDKmvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKfipKRGKSEKEL---RNLRQEIEILRKLNHPNIIEMLDSFETKKEFVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVD---HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPG 155
Cdd:cd14002   78 VTEYAQgelFQILEDDGTLPE----EEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdIDQLYHIMMclgnliprhqelfnKNPVf 235
Cdd:cd14002  154 LVLTSIKGTPLYMAPE-LVQEQPYDHTADLWSLGCILYELFVGQPPFYTNS-IYQLVQMIV--------------KDPV- 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 236 agvrlpeikereplerRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14002  217 ----------------KWPSnMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPF 252
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
9-347 6.35e-52

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 182.93  E-value: 6.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLEsddDKMVKKiamREIKLLKQLRHENLVNLLE------VCKKKKRWYL--VF 80
Cdd:PTZ00036  73 IIGNGSFGVVYEAICIDTSEKVAIKKVLQ---DPQYKN---RELLIMKNLNHINIIFLKDyyytecFKKNEKNIFLnvVM 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFP---NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS-QSGVVKLCDFGFARTLAApGE 156
Cdd:PTZ00036 147 EFIPQTVHKYMKHYArnnHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSAKNLLA-GQ 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQELFNKNPVFA 236
Cdd:PTZ00036 226 RSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGT--PTEDQLKEMNPNYA 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 237 GVRLPEIKEREpLERRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ------------MDGFAERFS---QEL 300
Cdd:PTZ00036 304 DIKFPDVKPKD-LKKVFPKgTPDDAINFISQFLKYEPLKRLNPIEALADPFFDdlrdpciklpkyIDKLPDLFNfcdAEI 382
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 301 QlKVQKDARNVSLSKKSQNRKKE----KEKDDSLVEERKTLVVQDTNADPK 347
Cdd:PTZ00036 383 K-EMSDACRRKIIPKCTYEAYKEflmsDENDANIIADKISKDFGESNIDAK 432
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
3-287 1.76e-50

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 173.80  E-value: 1.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDL--------ELFPnglDYQVVqKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd08215   81 ADGGDLAQKikkqkkkgQPFP---EEQIL-DWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLEST 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDsdidqlyhimmclgNLiprhQELFNKnpv 234
Cdd:cd08215  157 TDLAKTVVGTPYYLSPELCENK-PYNYKSDIWALGCVLYELCTLKHPFEAN--------------NL----PALVYK--- 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 235 fagvrlpeI--KEREPLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd08215  215 --------IvkGQYPPIPSQY---SSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
3-286 3.65e-50

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 179.05  E-value: 3.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLE--SDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:COG0515    8 RYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPelAADPEARERF-RREARALARLNHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLeLFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:COG0515   87 EYVEGESLADL-LRRRGpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVA-TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfnknpvfagv 238
Cdd:COG0515  166 GTVVgTPGYMAPEQARGE-PVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLR---------------------- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 239 rlpeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:COG0515  223 -----EPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAAAL 265
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
2-287 6.75e-50

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 174.85  E-value: 6.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV------CKKKKR 75
Cdd:cd07878   15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVftpatsIENFNE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHTILDDLELfpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlaaPG 155
Cdd:cd07878   95 VYLVTNLMGADLNNIVKC--QKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQ---AD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIPrhqELFNKNPVF 235
Cdd:cd07878  170 DEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSP---EVLKKISSE 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 236 AGVR----LPEIKEREpLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07878  247 HARKyiqsLPHMPQQD-LKKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYF 301
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
3-287 7.55e-50

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 172.00  E-value: 7.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmvKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKInLESKEKK--ESIL-NEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaAPGEVYTD 160
Cdd:cd05122   78 FCSGGSLKDlLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQL-SDGKTRNT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnliprhqelfnKNPVfagvrl 240
Cdd:cd05122  157 FVGTPYWMAPEVIQGK-PYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIA---------------TNGP------ 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 241 PEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd05122  215 PGLRNPK-------KWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
3-284 2.27e-49

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 173.37  E-value: 2.27e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW------ 76
Cdd:cd07850    1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDDLELfpnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlAAPGE 156
Cdd:cd07850   81 YLVMELMDANLCQVIQM---DLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-AGTSF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGN--------LIPRHQEL 228
Cdd:cd07850  157 MMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTpsdefmsrLQPTVRNY 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 229 FNKNPVFAGVRLPEI-------KEREPLERRYPklsEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd07850  236 VENRPKYAGYSFEELfpdvlfpPDSEEHNKLKA---SQARDLLSKMLVIDPEKRISVDDALQH 295
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
3-288 2.97e-49

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 170.47  E-value: 2.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06614    1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMrLRKQNKELIIN----EILIMKECKHPNIVDYYDSYLVGDELWVVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd06614   77 YMDGGSLTDiITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqelfNKNPVfagvrl 240
Cdd:cd06614  157 VVGTPYWMAPE-VIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLI---------------TTKGI------ 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 241 PEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06614  215 PPLKNPE-------KWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
4-287 1.47e-48

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 168.60  E-value: 1.47e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKkflesdddkMVKKI------AMREIKLLKQLR------HENLVNLLEVCK 71
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALK---------IIKNNkdyldqSLDEIRLLELLNkkdkadKYHIVRLKDVFY 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  72 KKKRWYLVFEFVDHTILDDLE--LFPnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG--VVKLCDFGF 147
Cdd:cd14133   72 FKNHLCIVFELLSQNLYEFLKqnKFQ-YLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 148 ARTLaaPGEVYTdYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnLIPRHqe 227
Cdd:cd14133  151 SCFL--TQRLYS-YIQSRYYRAPEVILG-LPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIG-IPPAH-- 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 228 LFNKNPVfagvrlpeikereplerRYPKLsevvIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14133  224 MLDQGKA-----------------DDELF----VDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
10-283 1.50e-48

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 168.10  E-value: 1.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKdtGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVAT-RWy 167
Cdd:cd13999   79 DLLHKKKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTpRW- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 168 RAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGdsdidqlyhimmclgnliprhqelfnKNPVFAGVRLPEIKERE 247
Cdd:cd13999  158 MAPEVLRGE-PYTEKADVYSFGIVLWELLTGEVPFKE--------------------------LSPIQIAAAVVQKGLRP 210
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 578809600 248 PLerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd13999  211 PI---PPDCPPELSKLIKRCWNEDPEKRPSFSEIVK 243
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
1-288 5.93e-48

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 168.49  E-value: 5.93e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdddKMVKKIAM-REIKLLKQLR-HENLVNLLEVCK--KKKRW 76
Cdd:cd14132   17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVL------KPVKKKKIkREIKILQNLRgGPNIVKLLDVVKdpQSKTP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTilDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG-VVKLCDFGfartLAA-- 153
Cdd:cd14132   91 SLIFEYVNNT--DFKTLYPT-LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKrKLRLIDWG----LAEfy 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 -PGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEM-FMGEPLFPGDSDIDQLYHIMMCLGNliprhQELF-- 229
Cdd:cd14132  164 hPGQEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMiFRKEPFFHGHDNYDQLVKIAKVLGT-----DDLYay 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 230 -NKnpvfAGVRLPE-------IKEREPLERRYP-----KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14132  239 lDK----YGIELPPrlndilgRHSKKPWERFVNsenqhLVTPEALDLLDKLLRYDHQERITAKEAMQHPYFD 306
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
9-286 2.17e-47

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 165.65  E-value: 2.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM----VKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd06632    7 LLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDDKKsresVKQL-EQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 ----HTILDDLELFPngldYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTd 160
Cdd:cd06632   86 ggsiHKLLQRYGAFE----EPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKS- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVG-DVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIDQLyhimmclgnliprhQELFNknpVFAGVR 239
Cdd:cd06632  161 FKGSPYWMAPEVIMQkNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGV--------------AAIFK---IGNSGE 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 240 LPEIKEreplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06632  221 LPPIPD---------HLSPDAKDFIRLCLQRDPEDRPTASQLLEHPF 258
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
7-287 4.50e-47

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 164.32  E-value: 4.50e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LG-LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD- 84
Cdd:cd06627    4 LGdLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVEn 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 ---HTILDDLELFPNGLdyqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06627   84 gslASIIKKFGKFPESL----VAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPEL--LVGdvkYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlyhimmclgnliprhqelFNKNPVFAGVR 239
Cdd:cd06627  160 VGTPYWMAPEVieMSG---VTTASDIWSVGCTVIELLTGNPPY--------------------------YDLQPMAALFR 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 240 LpeIKEREPlerRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06627  211 I--VQDDHP---PLPEnISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
10-286 5.75e-47

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 164.40  E-value: 5.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEIrFQDNDPKTIKEIA-DEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR------TLAAPGEVYtDYV 162
Cdd:cd06626   87 EELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVklknntTTMAPGEVN-SLV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDVK--YGKAVDVWAIGCLVTEMFMGEPLFpgdSDIDQLYHIMMCLGNLIPrhqelfnknpvfagvrl 240
Cdd:cd06626  166 GTPAYMAPEVITGNKGegHGRAADIWSLGCVVLEMATGKRPW---SELDNEWAIMYHVGMGHK----------------- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 241 PEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06626  226 PPIPDSL-------QLSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
11-276 1.77e-46

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 163.10  E-value: 1.77e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    11 GEGSYGMVMKCR----NKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:smart00221   8 GEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDASEQQIEEF-LREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    87 ILDD--LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEVYTDYVAT 164
Cdd:smart00221  87 DLLDylRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL----YDDDYYKVK 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   165 ------RWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYHIMmclgnliprhqelfnknpvfAG 237
Cdd:smart00221 163 ggklpiRWM-APESLK-EGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLK--------------------KG 220
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 578809600   238 VRLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:smart00221 221 YRLP----------KPPNCPPELYKLMLQCWAEDPEDRP 249
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
11-288 2.10e-46

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 162.64  E-value: 2.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKFLESD--DDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH--- 85
Cdd:cd14007    9 GKGKFGNVYLAREKKSGFIVALKVISKSQlqKSGLEHQLR-REIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNgel 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 -TILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlaAPGEVYTDYVAT 164
Cdd:cd14007   88 yKELKKQKRFDE----KEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH--APSNRRKTFCGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprHQELFNKnpvfagvrlpeIK 244
Cdd:cd14007  162 LDYLPPEMVEGKE-YDYKVDIWSLGVLCYELLVGKPPFESKS------------------HQETYKR-----------IQ 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 245 EREPlerRYP-KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14007  212 NVDI---KFPsSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
5-289 3.56e-46

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 162.38  E-value: 3.56e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQL-LRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 ----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHS-HNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd06623   83 ggslADLLKKVGKIPE----PVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGE-PLFPGDSD--IDQLYHIMMClgnliprhqelfnknpvfa 236
Cdd:cd06623  159 TFVGTVTYMSPERIQGE-SYSYAADIWSLGLTLLECALGKfPFLPPGQPsfFELMQAICDG------------------- 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 237 gvrlpeikerEPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06623  219 ----------PPPSLPAEEFSPEFRDFISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
3-288 5.07e-46

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 164.57  E-value: 5.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKR------- 75
Cdd:cd07854    6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQSV--KHALREIKIIRRLDHDNIVKVYEVLGPSGSdltedvg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 -------WYLVFEFVDHTILDDLELFPNGLDYqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG-VVKLCDFGF 147
Cdd:cd07854   84 sltelnsVYIVQEYMETDLANVLEQGPLSEEH--ARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDlVLKIGDFGL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 148 ARTLAaPGEVYTDY----VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQlyhiMMCLGNLIP 223
Cdd:cd07854  162 ARIVD-PHYSHKGYlsegLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQ----MQLILESVP 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 224 -----RHQELFNKNPVFAGVRLPEIkeREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07854  237 vvreeDRNELLNVIPSFVRNDGGEP--RRPLRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
10-284 8.00e-46

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 161.55  E-value: 8.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR---NKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd00192    3 LGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDASESERKDF-LKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDD---------LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEV 157
Cdd:cd00192   82 DLLDflrksrpvfPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDI----YD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTDYVAT-------RWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYHIMmclgnliprhqelf 229
Cdd:cd00192  158 DDYYRKKtggklpiRWM-APESLK-DGIFTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEVLEYLR-------------- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 230 nknpvfAGVRLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd00192  222 ------KGYRLP----------KPENCPDELYELMLSCWQLDPEDRPTFSELVER 260
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
11-276 9.17e-46

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 161.16  E-value: 9.17e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    11 GEGSYGMVMKCR----NKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:smart00219   8 GEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQIEEF-LREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    87 ILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEVYTDYVAT- 164
Cdd:smart00219  87 DLLSyLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL----YDDDYYRKRg 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   165 -----RWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYHIMmclgnliprhqelfnknpvfAGV 238
Cdd:smart00219 163 gklpiRWM-APESLK-EGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLK--------------------NGY 220
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 578809600   239 RLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:smart00219 221 RLP----------QPPNCPPELYDLMLQCWAEDPEDRP 248
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
10-288 4.01e-45

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 162.61  E-value: 4.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKK-----KRWYLVFEFVd 84
Cdd:cd07853    8 IGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPhidpfEEIYVVTELM- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY-TDYVA 163
Cdd:cd07853   87 QSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKHmTQEVV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliPRHQELFN-----KNPVFAGV 238
Cdd:cd07853  167 TQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGT--PSLEAMRSacegaRAHILRGP 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 239 RLPeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd07853  245 HKP--PSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAADALAHPYLD 292
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
10-287 2.94e-44

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 156.91  E-value: 2.94e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKI----AMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD- 84
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVL---RKKEIIKRKevehTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPg 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 ---HTILDDLELFPNGldyqVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd05123   78 gelFSHLSKEGRFPEE----RARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprHQELFNKnpvfagvrlp 241
Cdd:cd05123  154 CGTPEYLAPEVLLG-KGYGKAVDWWSLGVLLYEMLTGKPPFYAEN------------------RKEIYEK---------- 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 242 eIKEREPlerRYP-KLSEVVIDLAKKCLHIDPDKRPFCA---ELLHHDFF 287
Cdd:cd05123  205 -ILKSPL---KFPeYVSPEAKSLISGLLQKDPTKRLGSGgaeEIKAHPFF 250
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
1-289 9.41e-44

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 158.71  E-value: 9.41e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW---- 76
Cdd:cd07874   16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefq 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 --YLVFEFVDHTILDDLELfpnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlAAP 154
Cdd:cd07874   96 dvYLVMELMDANLCQVIQM---ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-AGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGN--------LIPRHQ 226
Cdd:cd07874  172 SFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTpcpefmkkLQPTVR 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 227 ELFNKNPVFAGVRLPEIKERE--PLERRYPKL-SEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd07874  251 NYVENRPKYAGLTFPKLFPDSlfPADSEHNKLkASQARDLLSKMLVIDPAKRISVDEALQHPYINV 316
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
1-289 1.04e-43

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 158.65  E-value: 1.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW---- 76
Cdd:cd07876   20 LKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLeefq 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 --YLVFEFVDHTILDDLELfpnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlAAP 154
Cdd:cd07876  100 dvYLVMELMDANLCQVIHM---ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-ACT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGN--------LIPRHQ 226
Cdd:cd07876  176 NFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTpsaefmnrLQPTVR 254
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 227 ELFNKNPVFAGVRLPEIKERE--PLERRYPKL-SEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd07876  255 NYVENRPQYPGISFEELFPDWifPSESERDKLkTSQARDLLSKMLVIDPDKRISVDEALRHPYITV 320
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
10-284 4.50e-42

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 151.11  E-value: 4.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   10 VGEGSYGMVMKCR----NKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:pfam07714   7 LGEGAFGEVYKGTlkgeGENTKIKVAVKTLKEGADEEEREDF-LEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   86 TILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD---Y 161
Cdd:pfam07714  86 GDLLDfLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYDDDYYRKRgggK 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  162 VATRWYrAPELLvgdvKYGK---AVDVWAIGCLVTEMF-MGEPLFPGDSDidqlyhimmclgnliprhQELFNKnpVFAG 237
Cdd:pfam07714 166 LPIKWM-APESL----KDGKftsKSDVWSFGVLLWEIFtLGEQPYPGMSN------------------EEVLEF--LEDG 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 578809600  238 VRLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:pfam07714 221 YRLP----------QPENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
10-287 1.62e-41

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 150.44  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK----KFLeSDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05581    9 LGEGSYSTVVLAKEKETGKEYAIKvldkRHI-IKEKKV--KYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVLEYAPN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 -TILDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL------------- 151
Cdd:cd05581   86 gDLLEYIRKYGS-LDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLgpdsspestkgda 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPGEVYTD----YVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlYHIMmclgnliprhQE 227
Cdd:cd05581  165 DSQIAYNQAraasFVGTAEYVSPELL-NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNE----YLTF----------QK 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 228 LFNKNPVFAgvrlpeikereplerryPKLSEVVIDLAKKCLHIDPDKRPFCA------ELLHHDFF 287
Cdd:cd05581  230 IVKLEYEFP-----------------ENFPPDAKDLIQKLLVLDPSKRLGVNenggydELKAHPFF 278
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
2-287 1.75e-41

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 149.72  E-value: 1.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIK----EISILKQCDSPYIVKYYGSYFKNTDLWIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVD-HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd06612   79 YCGaGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIdqlyHIMMCLgNLIPrhqelfNKNPvfagvrl 240
Cdd:cd06612  159 VIGTPFWMAPEVI-QEIGYNNKADIWSLGITAIEMAEGKPPY---SDI----HPMRAI-FMIP------NKPP------- 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 241 PEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06612  217 PTLSDPE-------KWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
4-287 4.21e-41

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 150.86  E-value: 4.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKkflesdddkMVK------KIAMREIKLLKQLR-------HENLVNLLE-- 68
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVK---------VLKnkpayfRQAMLEIAILTLLNtkydpedKHHIVRLLDhf 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 -----VCkkkkrwyLVFEfvdhtiLDDLELFP-------NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ 136
Cdd:cd14212   72 mhhghLC-------IVFE------LLGVNLYEllkqnqfRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 137 --SGVVKLCDFGFA----RTlaapgeVYTdYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQ 210
Cdd:cd14212  139 ldSPEIKLIDFGSAcfenYT------LYT-YIQSRFYRSPEVLLG-LPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQ 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 211 LYHIMMCLGNLiPRH--------QELFNKNPVFAGVRLPEIKEREPLERR-------------YPKLSEVV--------- 260
Cdd:cd14212  211 LSRIIEMLGMP-PDWmlekgkntNKFFKKVAKSGGRSTYRLKTPEEFEAEnncklepgkryfkYKTLEDIImnypmkksk 289
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 578809600 261 --------------IDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14212  290 keqidkemetrlafIDFLKGLLEYDPKKRWTPDQALNHPFI 330
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
1-288 9.50e-41

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 150.16  E-value: 9.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK------KFLESdddkmvkkiAMREIKLLKQL-RHENLVNLLEVckKK 73
Cdd:cd14226   12 MDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKiiknkkAFLNQ---------AQIEVRLLELMnKHDTENKYYIV--RL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWY-------LVFEFVDHTILDdleLFPN----GLDYQVVQKYLFQIINGIGFCHSH--NIIHRDIKPENILV--SQSG 138
Cdd:cd14226   81 KRHFmfrnhlcLVFELLSYNLYD---LLRNtnfrGVSLNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLcnPKRS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 139 VVKLCDFGFARTLaapGEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCL 218
Cdd:cd14226  158 AIKIIDFGSSCQL---GQRIYQYIQSRFYRSPEVLLG-LPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 219 GnLIPRH--------QELFNKNPVFAGVRLPEIKEREPLERRYPKLSEVV-------------------------IDLAK 265
Cdd:cd14226  234 G-MPPVHmldqapkaRKFFEKLPDGTYYLKKTKDGKKYKPPGSRKLHEILgvetggpggrragepghtvedylkfKDLIL 312
                        330       340
                 ....*....|....*....|...
gi 578809600 266 KCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14226  313 RMLDYDPKTRITPAEALQHSFFK 335
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
10-286 1.28e-40

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 146.98  E-value: 1.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKkflESDDDKMVKKIA---MREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDht 86
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIK---EISRKKLNKKLQenlESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCA-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 iLDDLELF---PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLAApgevyTD 160
Cdd:cd14009   76 -GGDLSQYirkRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKIADFGFARSLQP-----AS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVAT----RWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIdQLYHIMMCLGNLIPRHqelfnknpvfa 236
Cdd:cd14009  150 MAETlcgsPLYMAPEILQFQ-KYDAKADLWSVGAILFEMLVGKPPFRGSNHV-QLLRNIERSDAVIPFP----------- 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 237 gvrlpeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14009  217 ---------------IAAQLSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-287 3.32e-40

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 146.53  E-value: 3.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkflESDDDKMV---KKIAMREIKLLKQLRHENLVNLL--EVCKKKKRWY 77
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWK---EIDYGKMSekeKQQLVSEVNILRELKHPNIVRYYdrIVDRANTTLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHtilDDLELFPNG-------LDYQVVQKYLFQIINGIGFCHSHN-----IIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd08217   78 IVMEYCEG---GDLAQLIKKckkenqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARTLAAPGEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprH 225
Cdd:cd08217  155 GLARVLSHDSSFAKTYVGTPYYMSPELL-NEQSYDEKSDIWSLGCLIYELCALHPPFQAAN------------------Q 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 226 QELFNKnpvfagvrlpeIKE--REPLERRY-PKLSEVVidlaKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd08217  216 LELAKK-----------IKEgkFPRIPSRYsSELNEVI----KSMLNVDPDKRPSVEELLQLPLI 265
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
1-289 5.90e-40

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 148.65  E-value: 5.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW---- 76
Cdd:cd07875   23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefq 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 --YLVFEFVDHTILDDLELfpnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlAAP 154
Cdd:cd07875  103 dvYIVMELMDANLCQVIQM---ELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART-AGT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGN--------LIPRHQ 226
Cdd:cd07875  179 SFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTpcpefmkkLQPTVR 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 227 ELFNKNPVFAGVRLPEIKERE--PLERRYPKL-SEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd07875  258 TYVENRPKYAGYSFEKLFPDVlfPADSEHNKLkASQARDLLSKMLVIDASKRISVDEALQHPYINV 323
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
3-287 1.26e-39

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 146.21  E-value: 1.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTG-RIVAIKkFLESDDdkMVKKIAMREIKLLKQL--------RHenLVNLLEVCKKK 73
Cdd:cd14135    1 RYRVYGYLGKGVFSNVVRARDLARGnQEVAIK-IIRNNE--LMHKAGLKELEILKKLndadpddkKH--CIRLLRHFEHK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHTILDDLELFPN--GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFART 150
Cdd:cd14135   76 NHLCLVFESLSMNLREVLKKYGKnvGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKkNTLKLCDFGSASD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 lAAPGEVyTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----NLIPRHQ 226
Cdd:cd14135  156 -IGENEI-TPYLVSRFYRAPEIILG-LPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGkfpkKMLRKGQ 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 227 ---ELFNKNPVFAGVRLPEIKERE------------PLERR-----------YPKLSEVViDLAKKCLHIDPDKRPFCAE 280
Cdd:cd14135  233 fkdQHFDENLNFIYREVDKVTKKEvrrvmsdikptkDLKTLligkqrlpdedRKKLLQLK-DLLDKCLMLDPEKRITPNE 311

                 ....*..
gi 578809600 281 LLHHDFF 287
Cdd:cd14135  312 ALQHPFI 318
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
9-287 1.90e-39

Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MEKK3, MEKK2, and related proteins; all contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKK) that activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 144.04  E-value: 1.90e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIAM--REIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTGRELAVKQVeIDPINTEASKEVKAleCEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 -TILDDLELFpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA--PGEVYTDYV 162
Cdd:cd06625   87 gSVKDEIKAY-GALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTicSSTGMKSVT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfnKNPVFagvRLPe 242
Cdd:cd06625  166 GTPYWMSPEVINGE-GYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAT--------------QPTNP---QLP- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 243 ikereplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06625  227 -----------PHVSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
9-275 1.41e-38

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 141.70  E-value: 1.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF----LESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd14069    8 TLGEGAFGEVFLAVNRNTEEAVAVKFVdmkrAPGDCPENIKK----EVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYAS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE--VYTDYV 162
Cdd:cd14069   84 GGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRYKGKerLLNKMC 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEplFPGD--SDIDQLYhimmclgnliprHQELFNKNpvfagvrl 240
Cdd:cd14069  164 GTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGE--LPWDqpSDSCQEY------------SDWKENKK-------- 221
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 578809600 241 peikerePLERRYPKLSEVVIDLAKKCLHIDPDKR 275
Cdd:cd14069  222 -------TYLTPWKKIDTAALSLLRKILTENPNKR 249
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
2-287 2.45e-38

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 141.15  E-value: 2.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESD--DDKMVKKIAMrEIKLLKQLRHENLVnllevckkkkRWYLV 79
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSltKPKQREKLKS-EIKIHRSLKHPNIV----------KFHDC 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHT-ILddLELFPNG--LDYQVVQK---------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGF 147
Cdd:cd14099   70 FEDEENVyIL--LELCSNGslMELLKRRKaltepevryFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 148 ARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGdSDIDQLYHimmclgnliprhqe 227
Cdd:cd14099  148 AARLEYDGERKKTLCGTPNYIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFET-SDVKETYK-------------- 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 228 lfnknpvfagvrlpEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14099  213 --------------RIKKNEYSFPSHLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
9-286 1.05e-37

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 139.82  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF------LESDDDKMVKKI-AMR-EIKLLKQLRHENLVNllevckkkkrwYLVF 80
Cdd:cd06629    8 LIGKGTYGRVYLAMNATTGEMLAVKQVelpktsSDRADSRQKTVVdALKsEIDTLKDLDHPNIVQ-----------YLGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNG-----------LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd06629   77 EETEDYFSIFLEYVPGGsigsclrkygkFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAapgEVYTDYVATR-----WYRAPELLVGDVK-YGKAVDVWAIGCLVTEMFMGEPLFPGDsdidQLYHIMMCLGNLip 223
Cdd:cd06629  157 KSD---DIYGNNGATSmqgsvFWMAPEVIHSQGQgYSAKVDIWSLGCVVLEMLAGRRPWSDD----EAIAAMFKLGNK-- 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 224 rhqelfnknpvfagVRLPEIKEReplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06629  228 --------------RSAPPVPED-------VNLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
5-289 1.07e-37

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 139.40  E-value: 1.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd06605    4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQI-LRELDVLHKCNSPYIVGFYGAFYSEGDISICMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHS-HNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgEVYTDYVA 163
Cdd:cd06605   83 GGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVD--SLAKTFVG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG------EPLFPGDSDIDQLYHIMmclgnliprhqelfNKNPvfag 237
Cdd:cd06605  161 TRSYMAPERISGG-KYTVKSDIWSLGLSLVELATGrfpyppPNAKPSMMIFELLSYIV--------------DEPP---- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 238 VRLPEikereplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06605  222 PLLPS-----------GKFSPDFQDFVSQCLQKDPTERPSYKELMEHPFIKR 262
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
3-284 4.39e-37

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 137.99  E-value: 4.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAM--REIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLfqREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG--VVKLCDFGFARTLAApGEVY 158
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHT-GTFL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVG-----DVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQLYhimmclgNLIPR---HQELFN 230
Cdd:cd14098  160 VTFCGTMAYLAPEILMSkeqnlQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQ-LPVE-------KRIRKgryTQPPLV 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 231 KNpvfagvrlpeikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14098  232 DF----------------------NISEEAIDFILRLLDVDPEKRMTAAQALDH 263
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
10-286 1.04e-36

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 136.77  E-value: 1.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14074   11 LGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLEL-FPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFARTLaAPGEVYTDYVATRWY 167
Cdd:cd14074   91 DYIMkHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKF-QPGEKLETSCGSLAY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 168 RAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClGNLIPRHqelfnknpvfagvrlpeikere 247
Cdd:cd14074  170 SAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDC-KYTVPAH---------------------- 226
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 578809600 248 plerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14074  227 --------VSPECKDLIRRMLIRDPKKRASLEEIENHPW 257
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
13-287 1.53e-36

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 136.58  E-value: 1.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  13 GSYGMVMKCRNKDTGRIVAIKKFLESD-DDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD----HTI 87
Cdd:cd05579    4 GAYGRVYLAKKKSTGDLYAIKVIKKRDmIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPggdlYSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLelfpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---------------TLA 152
Cdd:cd05579   84 LENV----GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvrrqiklsiqkkSNG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhQELFNKn 232
Cdd:cd05579  160 APEKEDRRIVGTPDYLAPEILLGQ-GHGKTVDWWSLGVILYEFLVGIPPFHAETP------------------EEIFQN- 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 233 pvfagvrlpeIKER--EPLErrYPKLSEVVIDLAKKCLHIDPDKRPFC---AELLHHDFF 287
Cdd:cd05579  220 ----------ILNGkiEWPE--DPEVSDEAKDLISKLLTPDPEKRLGAkgiEEIKNHPFF 267
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
3-287 1.67e-36

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 138.30  E-value: 1.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLesdDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWY----- 77
Cdd:cd14225   44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIR---NKKRFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYfrnhl 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 -LVFEFVDhtiLDDLELFP----NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG--VVKLCDFGfaRT 150
Cdd:cd14225  121 cITFELLG---MNLYELIKknnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGqsSIKVIDFG--SS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTdYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnLIPRH--QEL 228
Cdd:cd14225  196 CYEHQRVYT-YIQSRFYRSPEVILG-LPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLG-LPPPEliENA 272
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 229 FNKNPVFAGVRLPEIKEREPLERRYP---KLSEVV-------IDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14225  273 QRRRLFFDSKGNPRCITNSKGKKRRPnskDLASALktsdplfLDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
9-286 1.74e-36

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 136.41  E-value: 1.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMkCRNKDTGRIVAIKKF-LESDD----DKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd06631    8 VLGKGAYGTVY-CGLTSTGQLIAVKQVeLDTSDkekaEKEYEKL-QEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 -DHTILDDLELFpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA------APGE 156
Cdd:cd06631   86 pGGSIASILARF-GALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCinlssgSQSQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclGN---LIPrhqelfnknp 233
Cdd:cd06631  165 LLKSMRGTPYWMAPE-VINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAI----GSgrkPVP---------- 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 234 vfagvRLPEikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06631  230 -----RLPD------------KFSPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
11-287 7.97e-36

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 134.30  E-value: 7.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIK-----KFLEsddDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDh 85
Cdd:cd14081   10 GKGQTGLVKLAKHCVTGQKVAIKivnkeKLSK---ESVLMKVE-REIAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVS- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 tildDLELFpnglDYQV---------VQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtLAAPGE 156
Cdd:cd14081   85 ----GGELF----DYLVkkgrltekeARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMAS-LQPEGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQLYHIMmclgnliprhqelfnKNPVFa 236
Cdd:cd14081  156 LLETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPF-DDDNLRQLLEKV---------------KRGVF- 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 237 gvRLPEIkereplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14081  219 --HIPHF------------ISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
11-284 8.79e-36

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 133.93  E-value: 8.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDhtildD 90
Cdd:cd14006    2 GRGRFGVVKRCIEKATGREFA-AKFIPKRDKK--KEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCS-----G 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  91 LELFPNGLDYQV-----VQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV--VKLCDFGFARTLaAPGEVYTDYVA 163
Cdd:cd14006   74 GELLDRLAERGSlseeeVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKL-NPGEELKEIFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLiprhqelfnKNPVFAGVrlpei 243
Cdd:cd14006  153 TPEFVAPEIVNGEP-VSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDF---------SEEYFSSV----- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 578809600 244 kereplerrypklSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14006  218 -------------SQEAKDFIRKLLVKEPRKRPTAQEALQH 245
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
10-287 1.06e-35

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 135.58  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTG--RIVAIKKFlesdDDKMVKKIAMREIKLLKQLRHENLVNLLEV--CKKKKRWYLVFEFVDH 85
Cdd:cd07867   10 VGRGTYGHVYKAKRKDGKdeKEYALKQI----EGTGISMSACREIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLELF--------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV----SQSGVVKLCDFGFARTLAA 153
Cdd:cd07867   86 DLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDY---VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFP-GDSDI--------DQLYHIMMCLGNL 221
Cdd:cd07867  166 PLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHcRQEDIktsnpfhhDQLDRIFSVMGFP 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 222 IPRHQELFNKNPVFAGVRLPEIKER-------EPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd07867  246 ADKDWEDIRKMPEYPTLQKDFRRTTyanssliKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 318
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
4-286 1.54e-35

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 135.27  E-value: 1.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAMREIKLLKQLRHE-----NLVNLLEVCKKKKRWYL 78
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL---KNHPSYARQGQIEVSILSRLSQEnadefNFVRAYECFQHKNHTCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDLE---LFPNGLDYqvVQKYLFQIINGIGFCHSHNIIHRDIKPENIL----VSQSGVVKLCDFGFARTL 151
Cdd:cd14211   78 VFEMLEQNLYDFLKqnkFSPLPLKY--IRPILQQVLTALLKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPgeVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnLIPRH------ 225
Cdd:cd14211  156 SKA--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQG-LPAEHllnaat 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 226 --QELFNKNP--VFAGVRL--PEIKERE----PLERR--------------YPK-------LSEVV-----IDLAKKCLH 269
Cdd:cd14211  232 ktSRFFNRDPdsPYPLWRLktPEEHEAEtgikSKEARkyifnclddmaqvnGPSdlegselLAEKAdrrefIDLLKRMLT 311
                        330
                 ....*....|....*..
gi 578809600 270 IDPDKRPFCAELLHHDF 286
Cdd:cd14211  312 IDQERRITPGEALNHPF 328
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
3-287 3.33e-35

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 132.51  E-value: 3.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESD-------DDKMVKKIAMrEIKLLKQLR---HENLVNLLEVCKK 72
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdtwvRDRKLGTVPL-EIHILDTLNkrsHPNIVKLLDFFED 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  73 KKRWYLVFEFVDHTI--LDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArT 150
Cdd:cd14004   80 DEFYYLVMEKHGSGMdlFDFIERKPN-MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA-A 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTdYVATRWYRAPELLVGDVKYGKAVDVWAIGCLvtemfmgeplfpgdsdidqLYHIMmclgnliprhqelFN 230
Cdd:cd14004  158 YIKSGPFDT-FVGTIDYAAPEVLRGNPYGGKEQDIWALGVL-------------------LYTLV-------------FK 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 231 KNPVFagvrlpEIKEREPLERRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14004  205 ENPFY------NIEEILEADLRIPYaVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
9-286 3.79e-35

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 132.66  E-value: 3.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVK-KIAM-----REIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKQVeLPSVSAENKDrKKSMldalqREIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVD----HTILDDLELFPNGLdyqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA------RTL 151
Cdd:cd06628   87 YVPggsvATLLNNYGAFEESL----VRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISkkleanSLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPGEVYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPgdsDIDQLYHIMMcLGNLIprhqelfnk 231
Cdd:cd06628  163 TKNNGARPSLQGSVFWMAPE-VVKQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFK-IGENA--------- 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 232 npvfagvrLPEIKereplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06628  229 --------SPTIP---------SNISSEARDFLEKTFEIDHNKRPTADELLKHPF 266
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
4-286 3.80e-35

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 132.53  E-value: 3.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLG---LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06624    7 YDESGervVLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREV--QPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELF---PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ-SGVVKLCDFGFARTLAAPGE 156
Cdd:cd06624   85 EQVPGGSLSALLRSkwgPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELL-VGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlyhimmclgnliprhQELfnKNPVF 235
Cdd:cd06624  165 CTETFTGTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPF-----------------------IEL--GEPQA 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 236 AGVRL------PEIKEreplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06624  220 AMFKVgmfkihPEIPE---------SLSEEAKSFILRCFEPDPDKRATASDLLQDPF 267
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
10-287 3.94e-35

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 132.31  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKC--RNKDTGRIVAIK---KFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd14080    8 IGEGSYSKVKLAeyTKSGLKEKVACKiidKKKAPKDF--LEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTildDLelfpngLDYqvVQKY----------LF-QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART-LA 152
Cdd:cd14080   86 HG---DL------LEY--IQKRgalsesqariWFrQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLcPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTD-YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQLYHIMMClgnliprhqelfnk 231
Cdd:cd14080  155 DDGDVLSKtFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPF-DDSNIKKMLKDQQN-------------- 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 232 npvfAGVRLPEIKEreplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14080  220 ----RKVRFPSSVK---------KLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
2-286 5.79e-35

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 132.37  E-value: 5.79e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdLEEAEDE-IEDIQ-QEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd06609   79 EYCGGGSVLDL-LKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKRNT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFpgdSDidqlYHIMMCLgNLIPRHqelfnkNPvfagvrl 240
Cdd:cd06609  158 FVGTPFWMAPEVIKQSG-YDEKADIWSLGITAIELAKGEPPL---SD----LHPMRVL-FLIPKN------NP------- 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 241 PEikerepLERRypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06609  216 PS------LEGN--KFSKPFKDFVELCLNKDPKERPSAKELLKHKF 253
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
2-288 6.91e-35

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 131.97  E-value: 6.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06647    7 KKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06647   85 YLAGGSLTDV-VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqelfnknpvfAGVRLP 241
Cdd:cd06647  164 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI---------------------ATNGTP 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 242 EIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06647  222 ELQNPE-------KLSAIFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
3-275 7.14e-35

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 131.70  E-value: 7.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLES-----DDDKMVKKIAMREIKLLKQL-RHENLVNLLEVCKKKKRW 76
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskDGNDFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTilddlELFPNGLDYQVVQ-------KYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFA 148
Cdd:cd13993   81 YIVLEYCPNG-----DLFEAITENRIYVgktelikNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 RTLAAPGEVytdYVATRWYRAPELL--VGDVKYG---KAVDVWAIG-CLVTEMFMGEP-LFPGDSDidqlyhimmclgnl 221
Cdd:cd13993  156 TTEKISMDF---GVGSEFYMAPECFdeVGRSLKGypcAAGDIWSLGiILLNLTFGRNPwKIASESD-------------- 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 222 iPRHQELFNKNPVFAGVrlpeikereplerrYPKLSEVVIDLAKKCLHIDPDKR 275
Cdd:cd13993  219 -PIFYDYYLNSPNLFDV--------------ILPMSDDFYNLLRQIFTVNPNNR 257
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
11-287 8.29e-35

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 131.23  E-value: 8.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKKIA------MREIKLLKQLRHENLVNLLEVC--KKKKRWYLVFEF 82
Cdd:cd14119    2 GEGSYGKVKEVLDTETLCRRAVKIL----KKRKLRRIPngeanvKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFP-NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA--APGEVYT 159
Cdd:cd14119   78 CVGGLQEMLDSAPdKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDlfAEDDTCT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDVKY-GKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmCLGNL-IPRHqelfnknpvfag 237
Cdd:cd14119  158 TSQGSPAFQPPEIANGQDSFsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENI--GKGEYtIPDD------------ 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 238 vrlpeikereplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14119  224 ------------------VDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
3-287 1.05e-34

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 131.27  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIkLEPGDDF---EIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06613   78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATIAKRKSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVK--YGKAVDVWAIGclVTEMFMGEpLFPGDSDIdqlyHIMMCLgNLIPRHqelfNKNPvfagvr 239
Cdd:cd06613  158 IGTPYWMAPEVAAVERKggYDGKCDIWALG--ITAIELAE-LQPPMFDL----HPMRAL-FLIPKS----NFDP------ 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 240 lPEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06613  220 -PKLKDKE-------KWSPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
4-288 1.05e-34

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 131.93  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdddKMVKKIAMREI-------KLLKQLRHENLVNLLEVCKKKKRW 76
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKIL------KKAKIIKLKQVehvlnekRILSEVRHPFIVNLLGSFQDDRNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLa 152
Cdd:cd05580   77 YMVMEYVPggelFSLLRRSGRFPN----DVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 aPGEVYTdYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDqLYhimmclgnliprhqelfnKN 232
Cdd:cd05580  152 -KDRTYT-LCGTPEYLAPEIILS-KGHGKAVDWWALGILIYEMLAGYPPFFDENPMK-IY------------------EK 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 233 PVFAGVRLPeikereplerryPKLSEVVIDLAKKCLHIDPDKR-----PFCAELLHHDFFQ 288
Cdd:cd05580  210 ILEGKIRFP------------SFFDPDAKDLIKRLLVVDLTKRlgnlkNGVEDIKNHPWFA 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
2-287 1.73e-34

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 130.94  E-value: 1.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK-------KFLESDDDKMVKKIaMREIKLLKQL-RHENLVNLLEVCKKK 73
Cdd:cd14093    3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKiiditgeKSSENEAEELREAT-RREIEILRQVsGHPNIIELHDVFESP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHTilddlELFpnglDY--QVV-------QKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCD 144
Cdd:cd14093   82 TFIFLVFELCRKG-----ELF----DYltEVVtlsekktRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 145 FGFARTLaAPGEVYTDYVATRWYRAPELLVGDV-----KYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlYH--IMMC 217
Cdd:cd14093  153 FGFATRL-DEGEKLRELCGTPGYLAPEVLKCSMydnapGYGKEVDMWACGVIMYTLLAGCPPF---------WHrkQMVM 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 218 LGNLIprhqelfNKNPVFAGvrlPEikereplerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14093  223 LRNIM-------EGKYEFGS---PE----------WDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
2-287 3.42e-34

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 131.92  E-value: 3.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkflesdddkMVKKI------AMREIKLLKQLRHE------NLVNLLEV 69
Cdd:cd14134   12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVK---------IIRNVekyreaAKIEIDVLETLAEKdpngksHCVQLRDW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  70 CKKKKRWYLVFEFVDHTILDDLELFpnglDYQV-----VQKYLFQIINGIGFCHSHNIIHRDIKPENIL----------- 133
Cdd:cd14134   83 FDYRGHMCIVFELLGPSLYDFLKKN----NYGPfplehVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlvdsdyvkvyn 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 134 --------VSQSGVVKLCDFG---FARtlaapgEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14134  159 pkkkrqirVPKSTDIKLIDFGsatFDD------EYHSSIVSTRHYRAPEVILG-LGWSYPCDVWSIGCILVELYTGELLF 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 203 PGDsdiDQLYHI-MM--CLGNLIPRH---------QELFNKNpvfaGVRLPE-------IKEREPLERRYPKLS----EV 259
Cdd:cd14134  232 QTH---DNLEHLaMMerILGPLPKRMirrakkgakYFYFYHG----RLDWPEgsssgrsIKRVCKPLKRLMLLVdpehRL 304
                        330       340
                 ....*....|....*....|....*...
gi 578809600 260 VIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14134  305 LFDLIRKMLEYDPSKRITAKEALKHPFF 332
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
10-287 3.92e-34

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 129.73  E-value: 3.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKC--RNKDTGRIVAIKKF----LESDDDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKR-WYLVFEF 82
Cdd:cd13994    1 IGKGATSVVRIVtkKNPRSGVLYAVKEYrrrdDESKRKDYVKRLT-SEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY- 161
Cdd:cd13994   80 CPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGMPAEKESPMs 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 ---VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNliprhqelfnknpvfagv 238
Cdd:cd13994  160 aglCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEKSGD------------------ 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 239 rlPEIKEREPLERRYPKLSEvviDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd13994  222 --FTNGPYEPIENLLPSECR---RLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-212 3.96e-34

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 129.45  E-value: 3.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESD---DDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIK-IIDKEqvaREGMVEQIK-REIAIMKLLRHPNIVELHEVMATKTKIFFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTilddlELF----PNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGF---ARTL 151
Cdd:cd14663   79 MELVTGG-----ELFskiaKNGrLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLsalSEQF 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 152 AAPGEVYTdYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLY 212
Cdd:cd14663  154 RQDGLLHT-TCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFD-DENLMALY 212
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
5-288 4.03e-34

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 130.25  E-value: 4.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVC-KKKKRWYLVFEFV 83
Cdd:cd06620    8 ETLKDLGAGNGGSVSKVLHIPTGTIMA-KKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFlNENNNIIICMEYM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHS-HNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYV 162
Cdd:cd06620   87 DCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELI--NSIADTFV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLIprhQELFNKNPvfagVRLPE 242
Cdd:cd06620  165 GTSTYMSPERIQGG-KYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLL---QRIVNEPP----PRLPK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 243 ikereplERRYPKLSEVVIDLakkCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06620  237 -------DRIFPKDLRDFVDR---CLLKDPRERPSPQLLLDHDPFI 272
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
4-286 5.36e-34

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 131.30  E-value: 5.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIamrEIKLLKQLRHEN-----LVNLLEVCKKKKRWYL 78
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQI---EVGILARLSNENadefnFVRAYECFQHRNHTCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDLE---LFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL----VSQSGVVKLCDFGFARTL 151
Cdd:cd14229   79 VFEMLEQNLYDFLKqnkFSP--LPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AApgEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG-------NLIPR 224
Cdd:cd14229  157 SK--TVCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGlpgeqllNVGTK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 225 HQELFNKNP--VFAGVRLPEIKEREP-------LERRY--PKLSEVV-----------------------IDLAKKCLHI 270
Cdd:cd14229  234 TSRFFCRETdaPYSSWRLKTLEEHEAetgmkskEARKYifNSLDDIAhvnmvmdlegsdllaekadrrefVALLKKMLLI 313
                        330
                 ....*....|....*.
gi 578809600 271 DPDKRPFCAELLHHDF 286
Cdd:cd14229  314 DADLRITPADTLSHPF 329
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
10-287 5.48e-34

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 131.33  E-value: 5.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTgrivaikkflESDDDKMVKKI--------AMREIKLLKQLRHENLVNLLEV--CKKKKRWYLV 79
Cdd:cd07868   25 VGRGTYGHVYKAKRKDG----------KDDKDYALKQIegtgismsACREIALLRELKHPNVISLQKVflSHADRKVWLL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELF--------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV----SQSGVVKLCDFGF 147
Cdd:cd07868   95 FDYAEHDLWHIIKFHraskankkPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 148 ARTLAAPGEVYTDY---VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFP-GDSDI--------DQLYHIM 215
Cdd:cd07868  175 ARLFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHcRQEDIktsnpyhhDQLDRIF 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 216 MCLG----------NLIPRHQEL---FNKNpVFAGVRLPEIKEREPLerrypKLSEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd07868  255 NVMGfpadkdwediKKMPEHSTLmkdFRRN-TYTNCSLIKYMEKHKV-----KPDSKAFHLLQKLLTMDPIKRITSEQAM 328

                 ....*
gi 578809600 283 HHDFF 287
Cdd:cd07868  329 QDPYF 333
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
2-287 8.24e-34

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 128.49  E-value: 8.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDT-------GRIVAIKKFLESDDDKMVkkiaMREIKLLKQLR-HENLVNLLEVCKKK 73
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSRI----LNELECLERLGgSNNVSGLITAFRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHtilDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS---QSGVvkLCDFGFART 150
Cdd:cd14019   77 DQVVAVLPYIEH---DDFRDFYRKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNretGKGV--LVDFGLAQR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIG----CLVTEMFmgePLFPGDSDIDQLYHIMMCLGnliprhq 226
Cdd:cd14019  152 EEDRPEQRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGvillSILSGRF---PFFFSSDDIDALAEIATIFG------- 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 227 elfnknpvfagvrlpeikereplerrypklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14019  222 ------------------------------SDEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
4-285 1.34e-33

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 128.64  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd14046    8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRI-LREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLelFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART-----LAAPGE 156
Cdd:cd14046   87 EKSTLRDL--IDSGLFQDTDRlwRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSnklnvELATQD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 V-------------YTDYVATRWYRAPELLVG-DVKYGKAVDVWAIGCLVTEMFmgeplFPGDSDIDQLyHIMMCLGNLI 222
Cdd:cd14046  165 InkstsaalgssgdLTGNVGTALYVAPEVQSGtKSTYNEKVDMYSLGIIFFEMC-----YPFSTGMERV-QILTALRSVS 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 223 PRHQELFNKNpvfagvrlpeikereplerRYPKLSEVVIDLakkcLHIDPDKRPFCAELLHHD 285
Cdd:cd14046  239 IEFPPDFDDN-------------------KHSKQAKLIRWL----LNHDPAKRPSAQELLKSE 278
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
4-286 1.78e-33

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 128.10  E-value: 1.78e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDtGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHE-NLVNLL--EVCKKKKRWYLVF 80
Cdd:cd14131    3 YEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGADEQTLQSYKNEIELLKKLKGSdRIIQLYdyEVTDEDDYLYMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDH---TILDdlELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPEN-ILVSqsGVVKLCDFGFARtlAAPGE 156
Cdd:cd14131   82 ECGEIdlaTILK--KKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVK--GRLKLIDFGIAK--AIQND 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 ---VYTD-YVATRWYRAPELLVGD---------VKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlYHIMmclgNLIP 223
Cdd:cd14131  156 ttsIVRDsQVGTLNYMSPEAIKDTsasgegkpkSKIGRPSDVWSLGCILYQMVYGKTPF---------QHIT----NPIA 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 224 RHQELFNKNPvfagvrlpEIKereplerrYPKLSE-VVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14131  223 KLQAIIDPNH--------EIE--------FPDIPNpDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
3-276 2.06e-33

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 127.77  E-value: 2.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESD-DDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEmMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDL--------ELFPNGldyqVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---- 149
Cdd:cd08224   81 LADAGDLSRLikhfkkqkRLIPER----TIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRffss 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 -TLAAPGEVYTDYvatrwYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdiDQLYhimmclgnliprhqEL 228
Cdd:cd08224  157 kTTAAHSLVGTPY-----YMSPERIREQ-GYDFKSDIWSLGCLLYEMAALQSPFYGEK--MNLY--------------SL 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 229 FNKnpvfagvrlpeIK--EREPL-ERRYpklSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd08224  215 CKK-----------IEkcEYPPLpADLY---SQELRDLVAACIQPDPEKRP 251
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
3-284 4.18e-33

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 129.87  E-value: 4.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAMREIKLLKQLRHE------NLVNLLEVCKKKKRW 76
Cdd:cd14224   66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMV---RNEKRFHRQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNHI 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDhtiLDDLELFP----NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV--VKLCDFGfaRT 150
Cdd:cd14224  143 CMTFELLS---MNLYELIKknkfQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG--SS 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTdYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLG----------- 219
Cdd:cd14224  218 CYEHQRIYT-YIQSRFYRAPEVILGA-RYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGmppqklletsk 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 220 ---NLI-----PRH---QELFNKNPVFAGVRLPEIKEREPLERRYPKLS------EVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd14224  296 rakNFIsskgyPRYctvTTLPDGSVVLNGGRSRRGKMRGPPGSKDWVTAlkgcddPLFLDFLKRCLEWDPAARMTPSQAL 375

                 ..
gi 578809600 283 HH 284
Cdd:cd14224  376 RH 377
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
4-282 4.31e-33

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 126.76  E-value: 4.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd08529   82 ENGDLHSLIKSQRGrpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAQTI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclGNLIPRhqelfnknpVFAGVrlp 241
Cdd:cd08529  162 VGTPYYLSPE-LCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQ-----------GALILK---------IVRGK--- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 578809600 242 eikeREPLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd08529  218 ----YPPISASY---SQDLSQLIDSCLTKDYRQRPDTTELL 251
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
2-288 4.70e-33

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 127.17  E-value: 4.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDD---DKMVkkiamrEIKLLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd06611    5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIqIESEEeleDFMV------EIDILSECKHPNIVGLYEAYFYENKLW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLEL-FPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd06611   79 ILIEFCDGGALDSIMLeLERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPlfpgdsdidqlyhimmclgnliPRHqelfNKN 232
Cdd:cd06611  159 KRDTFIGTPYWMAPEVVAcetfKDNPYDYKADIWSLGITLIELAQMEP----------------------PHH----ELN 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 233 PVfaGVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06611  213 PM--RVLLKILKSEPPTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
10-211 6.09e-33

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 126.57  E-value: 6.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESD--DDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD--- 84
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHivQTRQQEHI-FSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLgge 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 -HTILDDLELFpnglDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTdYVA 163
Cdd:cd05572   80 lWTILRDRGLF----DEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWT-FCG 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 164 TRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQL 211
Cdd:cd05572  155 TPEYVAPEIILN-KGYDFSVDYWSLGILLYELLTGRPPF-GGDDEDPM 200
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
2-287 1.42e-32

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 125.55  E-value: 1.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKI--AMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRI---DLEKCQTSMdeLRKEIQAMSQCNHPNVVSYYTSFVVGDELWLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDL--ELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd06610   78 MPLLSGGSLLDImkSSYPRGgLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 ----VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIDQLYHIMMCLGNLIPRHQElfnkn 232
Cdd:cd06610  158 rtrkVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPY---SKYPPMKVLMLTLQNDPPSLET----- 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 233 pvfagvrlpeikereplERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06610  230 -----------------GADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
11-287 2.19e-32

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 126.56  E-value: 2.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVdht 86
Cdd:cd05570    4 GKGSFGKVMLAERKKTDELYAIKvlkkEVIIEDDD--VECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYV--- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ilddlelfpNGLD--YQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd05570   79 ---------NGGDlmFHIQRARRFteerarfyaaEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhQELFNknpv 234
Cdd:cd05570  150 GNTTSTFCGTPDYIAPEILREQ-DYGFSVDWWALGVLLYEMLAGQSPFEGDDE------------------DELFE---- 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 235 fagvrlpEIKEREPLerrYPK-LSEVVIDLAKKCLHIDPDKRPFC-----AELLHHDFF 287
Cdd:cd05570  207 -------AILNDEVL---YPRwLSREAVSILKGLLTKDPARRLGCgpkgeADIKAHPFF 255
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
3-283 3.55e-32

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 124.75  E-value: 3.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvkKIAMREIKLLKQL-RHENLVNLL--EVCKKKKRW--Y 77
Cdd:cd13985    1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQL--RVAIKEIEIMKRLcGHPNIVQYYdsAILSSEGRKevL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLE-LFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd13985   79 LLMEYCPGSLVDILEkSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVA---------TRWYRAPEL--LVGDVKYGKAVDVWAIGCLvtemfmgeplfpgdsdidqLYHIMmclgnlip 223
Cdd:cd13985  159 LERAEEVNIieeeiqkntTPMYRAPEMidLYSKKPIGEKADIWALGCL-------------------LYKLC-------- 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 224 rhqelFNKNPVFAGVRLPEIKEREPLErRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd13985  212 -----FFKLPFDESSKLAIVAGKYSIP-EQPRYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
2-290 4.54e-32

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 125.53  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVK-KIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06633   21 EIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKwQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGevyTD 160
Cdd:cd06633  101 EYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA-SIASPA---NS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVG--DVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfNKNPVFagv 238
Cdd:cd06633  177 FVGTPYWMAPEVILAmdEGQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQ-------------NDSPTL--- 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 239 rlpEIKEREPLERRYpklsevvIDLakkCLHIDPDKRPFCAELLHHDFFQMD 290
Cdd:cd06633  241 ---QSNEWTDSFRGF-------VDY---CLQKIPQERPSSAELLRHDFVRRE 279
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-286 5.02e-32

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 124.51  E-value: 5.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmVKKIaMREIKLLKQLRH---ENLVNLLEVCKKKKRWYLV 79
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLnLDTDDDD-VSDI-QKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd06917   81 MDYCEGGSIRTL-MRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIDQLYHIMmclgnLIPRhqelfNKNPvfagvr 239
Cdd:cd06917  160 TFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPY---SDVDALRAVM-----LIPK-----SKPP------ 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 240 lpeikeREPLERRYPKLSEVVIdlakKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06917  221 ------RLEGNGYSPLLKEFVA----ACLDEEPKDRLSADELLKSKW 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
2-286 5.57e-32

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 123.95  E-value: 5.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDkMVKKIAMrEIKLLKQL-RHENLVNLLEVCKKKK------ 74
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIK-IMDIIED-EEEEIKL-EINILRKFsNHPNIATFYGAFIKKDppggdd 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVDHTILDDL----ELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd06608   83 QLWLVMEYCGGGSVTDLvkglRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTDYVATRWYRAPELLVG----DVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIdqlyHIMMCLgNLIPRhq 226
Cdd:cd06608  163 LDSTLGRRNTFIGTPYWMAPEVIACdqqpDASYDARCDVWSLGITAIELADGKPPL---CDM----HPMRAL-FKIPR-- 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 227 elfnkNPVfagvrlPEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06608  233 -----NPP------PTLKSPE-------KWSKEFNDFISECLIKNYEQRPFTEELLEHPF 274
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
4-285 8.45e-32

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 122.88  E-value: 8.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKK-----FLESDDDKmvkkiAMREIKLLKQL-RHENLVNLLEVCKKKKRWY 77
Cdd:cd13997    2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKskkpfRGPKERAR-----ALREVEAHAALgQHPNIVRYYSSWEEGGHLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDL--ELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd13997   77 IQMELCENGSLQDAleELSPISkLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTdyvATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLfpgdsdidqlyhimmclgnliPRHQELFNknpv 234
Cdd:cd13997  157 GDVEE---GDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGEPL---------------------PRNGQQWQ---- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 235 fagvrlpEIKE-REPLERRyPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd13997  209 -------QLRQgKLPLPPG-LVLSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
2-286 8.64e-32

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 124.07  E-value: 8.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVC--KKKKRWYLV 79
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFA-LKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFldEQDSSIGIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDL--ELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArtlaapG 155
Cdd:cd06621   80 MEYCEGGSLDSIykKVKKKGgrIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS------G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTD----YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSD-----IDQLYHIMmclgnliprhq 226
Cdd:cd06621  154 ELVNSlagtFTGTSYYMAPERIQGG-PYSITSDVWSLGLTLLEVAQNRFPFPPEGEpplgpIELLSYIV----------- 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 227 elfnKNPVfagvrlPEIKEREPLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06621  222 ----NMPN------PELKDEPENGIKW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPW 268
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
4-289 1.25e-31

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 125.20  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAMREIKLLKQLRHEN-----LVNLLEVCKKKKRWYL 78
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIL---KNHPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNHTCL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDLE---LFPNGLDYqvVQKYLFQIINGIGFCHSHNIIHRDIKPENIL----VSQSGVVKLCDFGFARTL 151
Cdd:cd14228   94 VFEMLEQNLYDFLKqnkFSPLPLKY--IRPILQQVATALMKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPgeVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnlIP-------- 223
Cdd:cd14228  172 SKA--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQG--LPaeyllsag 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 224 -RHQELFNKNPVFA----GVRLPE-------IKEREPLERRYPKLSEVV-----------------------IDLAKKCL 268
Cdd:cd14228  247 tKTSRFFNRDPNLGyplwRLKTPEeheletgIKSKEARKYIFNCLDDMAqvnmstdlegtdmlaekadrreyIDLLKKML 326
                        330       340
                 ....*....|....*....|.
gi 578809600 269 HIDPDKRPFCAELLHHDFFQM 289
Cdd:cd14228  327 TIDADKRITPLKTLNHPFVTM 347
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
2-287 1.71e-31

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 122.55  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKK-IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06648    7 SDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKM---DLRKQQRReLLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd06648   84 EFLEGGALTDIVTHTR-MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEVPRRKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlyhimmclgnliprhqelFNKNPVFAGVRl 240
Cdd:cd06648  163 LVGTPYWMAPE-VISRLPYGTEVDIWSLGIMVIEMVDGEPPY--------------------------FNEPPLQAMKR- 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 241 peIKEREPLERRYP-KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06648  215 --IRDNEPPKLKNLhKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
3-206 2.02e-31

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 122.11  E-value: 2.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIK--KFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14073    2 RYELLETLGKGTYGKVKLAIERATGREVAIKsiKKDKIEDEQDMVRI-RREIEIMSSLNHPHIIRIYEVFENKDKIVIVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGEVYTD 160
Cdd:cd14073   81 EYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS-NLYSKDKLLQT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 161 YVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd14073  160 FCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSD 205
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
3-287 2.71e-31

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 123.46  E-value: 2.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDddKMVKKIAMREIKLLKQLRH--------ENLVNLLE------ 68
Cdd:cd14136   11 RYHVVRKLGWGHFSTVWLCWDLQNKRFVALK-VVKSA--QHYTEAALDEIKLLKCVREadpkdpgrEHVVQLLDdfkhtg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 -----VCkkkkrwyLVFEFVDHTILDDLELF-PNGLDYQVVQKYLFQIINGIGFCHSH-NIIHRDIKPENILVSQSGV-V 140
Cdd:cd14136   88 pngthVC-------MVFEVLGPNLLKLIKRYnYRGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKIeV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 141 KLCDFGFARTLAAPgevYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLF---PGDS---DIDQLYHI 214
Cdd:cd14136  161 KIADLGNACWTDKH---FTEDIQTRQYRSPEVILG-AGYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 215 MMCLGNlIPRH--------QELFNKNPvfagvRLPEIKEREP------LERRYPKLSEVVIDLAK---KCLHIDPDKRPF 277
Cdd:cd14136  237 IELLGR-IPRSiilsgkysREFFNRKG-----ELRHISKLKPwpledvLVEKYKWSKEEAKEFASfllPMLEYDPEKRAT 310
                        330
                 ....*....|
gi 578809600 278 CAELLHHDFF 287
Cdd:cd14136  311 AAQCLQHPWL 320
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
9-287 3.24e-31

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 121.77  E-value: 3.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-----LESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd06630    7 LLGTGAFSSCYQARDVKTGTLMAVKQVsfcrnSSSEQEEVVEAI-REEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 D----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG-VVKLCDFGFARTLAA----P 154
Cdd:cd06630   86 AggsvASLLSKYGAFSE----NVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASkgtgA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPlfPGDSDIdqlyhimmclgnlIPRHQELFNKnpV 234
Cdd:cd06630  162 GEFQGQLLGTIAFMAPEVLRGE-QYGRSCDVWSVGCVIIEMATAKP--PWNAEK-------------ISNHLALIFK--I 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 235 FAGVRLPEIKEreplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd06630  224 ASATTPPPIPE---------HLSPGLRDVTLRCLELQPEDRPPARELLKHPVF 267
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
2-288 4.12e-31

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 121.40  E-value: 4.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVK-KIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06607    1 KIFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGevyTD 160
Cdd:cd06607   81 EYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA-SLVCPA---NS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPE--LLVGDVKYGKAVDVWAIGclVTEMFMGE---PLFPGDSdIDQLYHIMMclgnliprhqelfNKNPVF 235
Cdd:cd06607  157 FVGTPYWMAPEviLAMDEGQYDGKVDVWSLG--ITCIELAErkpPLFNMNA-MSALYHIAQ-------------NDSPTL 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 236 AGVrlpeikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06607  221 SSG----------------EWSDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
10-284 4.98e-31

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 121.23  E-value: 4.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDtGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14066    1 IGSGGFGTVYKGVLEN-GTVVAVKR-LNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLeLFPNG----LDYQVVQKYLFQIINGIGFCHSHN---IIHRDIKPENILVSQSGVVKLCDFGFAR--TLAAPGEVYTD 160
Cdd:cd14066   79 DR-LHCHKgsppLPWPQRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARliPPSESVSKTSA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG-EPLFPGDSDIDQLYHIMMCLGNLIPRHQELFNKNPvfagVR 239
Cdd:cd14066  158 VKGTIGYLAPEYIRTG-RVSTKSDVYSFGVVLLELLTGkPAVDENRENASRKDLVEWVESKGKEELEDILDKRL----VD 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 240 LPEIKEREPLErrypklsevVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14066  233 DDGVEEEEVEA---------LLRLALLCTRSDPSLRPSMKEVVQM 268
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
10-284 6.32e-31

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 121.31  E-value: 6.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAM------------------------REIKLLKQLRHENLVN 65
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKIL---SKKKLLKQAGFfrrppprrkpgalgkpldpldrvyREIAILKKLDHPNVVK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  66 LLEVCKK--KKRWYLVFEFVDH-TILDDLElfPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKL 142
Cdd:cd14118   79 LVEVLDDpnEDNLYMVFELVDKgAVMEVPT--DNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 143 CDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKY--GKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhiMMCLGN 220
Cdd:cd14118  157 ADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKfsGKALDIWAMGVTLYCFVFGRCPFEDDH--------ILGLHE 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 221 LIpRHQElfnknpvfagVRLPEikereplerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14118  229 KI-KTDP----------VVFPD----------DPVVSEQLKDLILRMLDKNPSERITLPEIKEH 271
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
2-287 1.01e-30

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 120.85  E-value: 1.01e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKM-------VKKIAMREIKLLKQLR-HENLVNLLEVCKKK 73
Cdd:cd14181   10 QKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVK-IIEVTAERLspeqleeVRSSTLKEIHILRQVSgHPSIITLIDSYESS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaA 153
Cdd:cd14181   89 TFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHL-E 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDVK-----YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliPRHQel 228
Cdd:cd14181  168 PGEKLRELCGTPGYLAPEILKCSMDethpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIME------GRYQ-- 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 229 fnknpvFAGvrlPEIKEReplerrypklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14181  240 ------FSS---PEWDDR----------SSTVKDLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
10-213 1.05e-30

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 120.09  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDdkMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14162    8 LGHGSYAVVKKAYSTKHKCKVAIKivsKKKAPED--YLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART--LAAPGEVY--TDYV 162
Cdd:cd14162   86 DLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGvmKTKDGKPKlsETYC 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 163 ATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQLYH 213
Cdd:cd14162  166 GSYAYASPEILRGIPYDPFLSDIWSMGVVLYTMVYGRLPF-DDSNLKVLLK 215
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
4-289 1.12e-30

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 122.51  E-value: 1.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAMREIKLLKQLRHE-----NLVNLLEVCKKKKRWYL 78
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL---KNHPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNHTCL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDLE---LFPNGLDYqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILV----SQSGVVKLCDFGFARTL 151
Cdd:cd14227   94 VFEMLEQNLYDFLKqnkFSPLPLKY--IRPILQQVATALMKLKSLGLIHADLKPENIMLvdpsRQPYRVKVIDFGSASHV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPgeVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGnlIP-------- 223
Cdd:cd14227  172 SKA--VCSTYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQG--LPaeyllsag 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 224 -RHQELFNKN-----PVFAgVRLPE-------IKEREPLERRYPKLSEVV-----------------------IDLAKKC 267
Cdd:cd14227  247 tKTTRFFNRDtdspyPLWR-LKTPEdheaetgIKSKEARKYIFNCLDDMAqvnmttdlegsdmlvekadrrefIDLLKKM 325
                        330       340
                 ....*....|....*....|..
gi 578809600 268 LHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd14227  326 LTIDADKRITPIETLNHPFVTM 347
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
2-289 1.75e-30

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 120.60  E-value: 1.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06655   19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPK--KELIINEILVMKELKNPNIVNFLDSFLVGDELFVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06655   97 YLAGGSLTDV-VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqelfnknpvfAGVRLP 241
Cdd:cd06655  176 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI---------------------ATNGTP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 242 EIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06655  234 ELQNPE-------KLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKL 274
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
2-289 2.55e-30

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 120.21  E-value: 2.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06656   19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06656   97 YLAGGSLTDV-VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqelfnknpvfAGVRLP 241
Cdd:cd06656  176 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI---------------------ATNGTP 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 242 EIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06656  234 ELQNPE-------RLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKL 274
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
2-289 2.83e-30

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 119.83  E-value: 2.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06654   20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPK--KELIINEILVMRENKNPNIVNYLDSYLVGDELWVVME 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06654   98 YLAGGSLTDV-VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTM 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqelfnknpvfAGVRLP 241
Cdd:cd06654  177 VGTPYWMAPE-VVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI---------------------ATNGTP 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 242 EIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06654  235 ELQNPE-------KLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKI 275
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
9-200 2.90e-30

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 118.97  E-value: 2.90e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIAMR--EIKLLKQLRHENLVNLLEVCK--KKKRWYLVFEFV 83
Cdd:cd06653    9 LLGRGAFGEVYLCYDADTGRELAVKQVpFDPDSQETSKEVNALecEIQLLKNLRHDRIVQYYGCLRdpEEKKLSIFVEYM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 -DHTILDDLELFpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---TLAAPGEVYT 159
Cdd:cd06653   89 pGGSVKDQLKAY-GALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriqTICMSGTGIK 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809600 160 DYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEP 200
Cdd:cd06653  168 SVTGTPYWMSPEVISGE-GYGRKADVWSVACTVVEMLTEKP 207
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
9-286 4.13e-30

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 118.61  E-value: 4.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKI-AMR-EIKLLKQLRHENLVNLLEVCKKKKRWYLVFeFVDH 85
Cdd:cd06652    9 LLGQGAFGRVYLCYDADTGRELAVKQVqFDPESPETSKEVnALEcEIQLLKNLLHERIVQYYGCLRDPQERTLSI-FMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 ----TILDDLELFpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---TLAAPGEVY 158
Cdd:cd06652   88 mpggSIKDQLKSY-GALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlqTICLSGTGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClgnliprhqelfNKNPVfagv 238
Cdd:cd06652  167 KSVTGTPYWMSPEVISGE-GYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQ------------PTNPQ---- 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 239 rLPeikereplerryPKLSEVVIDLAKKcLHIDPDKRPFCAELLHHDF 286
Cdd:cd06652  230 -LP------------AHVSDHCRDFLKR-IFVEAKLRPSADELLRHTF 263
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
11-287 5.40e-30

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 118.14  E-value: 5.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIK----KFLESDDdkMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14079   11 GVGSFGKVKLAEHELTGHKVAVKilnrQKIKSLD--MEEKIR-REIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ilddlELFpnglDYqVVQK---------YLF-QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGE 156
Cdd:cd14079   88 -----ELF----DY-IVQKgrlsedearRFFqQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS-NIMRDGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEplFPGDSDidqlyHIMMclgnliprhqeLFNK--NPV 234
Cdd:cd14079  157 FLKTSCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGS--LPFDDE-----HIPN-----------LFKKikSGI 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 235 FAgvrLPEikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14079  219 YT---IPS------------HLSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1-284 9.99e-30

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 117.37  E-value: 9.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM-VKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14116    4 LEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAgVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDH-TILDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFarTLAAPGEVY 158
Cdd:cd14116   84 LEYAPLgTVYRELQKLSK-FDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGW--SVHAPSSRR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprHQELFnknpvfagv 238
Cdd:cd14116  161 TTLCGTLDYLPPEMIEGRM-HDEKVDLWSLGVLCYEFLVGKPPFEANT------------------YQETY--------- 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 239 rlpeiKEREPLERRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14116  213 -----KRISRVEFTFPDfVTEGARDLISRLLKHNPSQRPMLREVLEH 254
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
4-287 2.15e-29

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 116.20  E-value: 2.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM--VKKIaMREIKLLKQLRHENLVNLlevckkkkrWYlvfE 81
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKdsVRNV-LNELEILQELEHPFLVNL---------WY---S 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHT---ILDDLeLFPNGLDYQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd05578   69 FQDEEdmyMVVDL-LLGGDLRYHLQQKvkfseetvkfYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 RTLaAPGEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSD--IDQLYHIMMCLGNLIPRHQ 226
Cdd:cd05578  148 TKL-TDGTLATSTSGTKPYMAPEVFMR-AGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRtsIEEIRAKFETASVLYPAGW 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 227 elfnknpvfagvrlpeikereplerrypklSEVVIDLAKKCLHIDPDKRPFC-AELLHHDFF 287
Cdd:cd05578  226 ------------------------------SEEAIDLINKLLERDPQKRLGDlSDLKNHPYF 257
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
2-285 2.90e-29

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 116.72  E-value: 2.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKKIA--MREIKLLKQLRHENLVNLLEVCKKKKR 75
Cdd:cd14084    6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKiinkRKFTIGSRREINKPRniETEIEILKKLSHPCIIKIEDFFDAEDD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLA 152
Cdd:cd14084   86 YYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSsqeEECLIKITDFGLSKILG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTdYVATRWYRAPELLV--GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhiMMCLGNLIPRHQELFN 230
Cdd:cd14084  166 ETSLMKT-LCGTPTYLAPEVLRsfGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYT-------QMSLKEQILSGKYTFI 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 231 KnpvfagvrlPEIKEreplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd14084  238 P---------KAWKN----------VSEEAKDLVKKMLVVDPSRRPSIEEALEHP 273
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-284 5.19e-29

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 116.37  E-value: 5.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTG-----RIVAIKKFLESDDDKMvkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd14086    9 LGKGAFSVVRRCVQKSTGqefaaKIINTKKLSARDHQKL-----EREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTilddlELFpnglDYQVVQKY---------LFQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFARTLA 152
Cdd:cd14086   84 GG-----ELF----EDIVAREFyseadashcIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQLYHIMMCLGNLIPrhqelfnkN 232
Cdd:cd14086  155 GDQQAWFGFAGTPGYLSPEVLRKD-PYGKPVDIWACGVILYILLVGYPPF-WDEDQHRLYAQIKAGAYDYP--------S 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 233 PVFAGVRlPEIKereplerrypklsevviDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14086  225 PEWDTVT-PEAK-----------------DLINQMLTVNPAKRITAAEALKH 258
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
2-286 7.02e-29

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 115.90  E-value: 7.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGrIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06644   12 EVWEIIGELGDGAFGKVYKAKNKETG-ALAAAKVIETKSEEELEDY-MVEIEILATCNHPYIVKLLGAFYWDGKLWIMIE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 F-----VDHTILDdlelFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd06644   90 FcpggaVDAIMLE----LDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELL----VGDVKYGKAVDVWAIGCLVTEMFMGEPlfPgdsdidqlyhimmclgnliprHQELfnkN 232
Cdd:cd06644  166 RRDSFIGTPYWMAPEVVmcetMKDTPYDYKADIWSLGITLIEMAQIEP--P---------------------HHEL---N 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 233 PVFAgvrLPEIKEREPLERRYP-KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06644  220 PMRV---LLKIAKSEPPTLSQPsKWSMEFRDFLKTALDKHPETRPSAAQLLEHPF 271
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
2-284 8.18e-29

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 116.10  E-value: 8.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTG-----RIVAIKKF-----LESDDDKmvkkiamREIKLLKQLRHENLVNLLEVCK 71
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRRCIHRETGqqfavKIVDVAKFtsspgLSTEDLK-------REASICHMLKHPHIVELLETYS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  72 KKKRWYLVFEFVDHTIL--DDLELFPNGLDYQ--VVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS---QSGVVKLCD 144
Cdd:cd14094   76 SDGMLYMVFEFMDGADLcfEIVKRADAGFVYSeaVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskeNSAPVKLGG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 145 FGFARTLAAPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdiDQLYHIMMclgnlipr 224
Cdd:cd14094  156 FGVAIQLGESGLVAGGRVGTPHFMAPEVVKRE-PYGKPVDVWGCGVILFILLSGCLPFYGTK--ERLFEGII-------- 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 225 hqelfnknpvfagvrlpeiKEREPLE-RRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14094  225 -------------------KGKYKMNpRQWSHISESAKDLVRRMLMLDPAERITVYEALNH 266
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
4-284 8.51e-29

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 114.66  E-value: 8.51e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAM--REIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKII---DKSKLKGKEDMieSEILIIKSLSHPNIVKLFEVYETEKEIYLILE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ----SGVVKLCDFGFARTLAAPgeV 157
Cdd:cd14185   79 YVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHnpdkSTTLKLADFGLAKYVTGP--I 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTdYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPG-DSDIDQLYHIMmclgnliprhqelfnknpvfa 236
Cdd:cd14185  157 FT-VCGTPTYVAPEILSEK-GYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQII--------------------- 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 237 gvrlpEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14185  214 -----QLGHYEFLPPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQH 256
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-288 1.19e-28

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 114.50  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDD--KMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIakNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlaapGEVY---TDYVAT 164
Cdd:cd05611   84 CASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRN----GLEKrhnKKFVGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPlfpgdsdidqlyhimmclgnliPRHQELFNKnpVFAGVRLPEIK 244
Cdd:cd05611  160 PDYLAPETILG-VGDDKMSDWWSLGCVIFEFLFGYP----------------------PFHAETPDA--VFDNILSRRIN 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 245 EReplERRYPKLSEVVIDLAKKCLHIDPDKR---PFCAELLHHDFFQ 288
Cdd:cd05611  215 WP---EEVKEFCSPEAVDLINRLLCMDPAKRlgaNGYQEIKSHPFFK 258
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
2-288 1.34e-28

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 114.63  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM-------VKKIAMREIKLLKQLR-HENLVNLLEVCKKK 73
Cdd:cd14182    3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFspeevqeLREATLKEIDILRKVSgHPNIIQLKDTYETN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaA 153
Cdd:cd14182   83 TFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQL-D 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDVK-----YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnliprhqel 228
Cdd:cd14182  162 PGEKLREVCGTPGYLAPEIIECSMDdnhpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIM------------- 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 229 fNKNPVFAGvrlPEIKEReplerrypklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14182  229 -SGNYQFGS---PEWDDR----------SDTVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-283 1.40e-28

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 114.70  E-value: 1.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVN-------------LLEVC 70
Cdd:cd13996    8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKV-LREVKALAKLNHPNIVRyytawveepplyiQMELC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  71 KKKKRWYLVfefvdhtildDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFAR 149
Cdd:cd13996   87 EGGTLRDWI----------DRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLAT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAPGE--------------VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMfmgepLFPGDSDIDQlYHIM 215
Cdd:cd13996  157 SIGNQKRelnnlnnnnngntsNNSVGIGTPLYASPEQLDGE-NYNEKADIYSLGIILFEM-----LHPFKTAMER-STIL 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 216 MCLGNLIprhqelfnknpvfagvrLPEIkerepLERRYPKlsevVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd13996  230 TDLRNGI-----------------LPES-----FKAKHPK----EADLIQSLLSKNPEERPSAEQLLR 271
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
4-284 1.69e-28

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 113.56  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVvQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYV 162
Cdd:cd14050   83 CDTSLQQYCEETHSLPESEV-WNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRwYRAPELLVGDvkYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLyhimmclgnlipRHQELfnknPvfagvrlpe 242
Cdd:cd14050  162 DPR-YMAPELLQGS--FTKAADIFSLGITILELACNLELPSGGDGWHQL------------RQGYL----P--------- 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 578809600 243 ikereplERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14050  214 -------EEFTAGLSPELRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
4-286 1.78e-28

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 114.08  E-value: 1.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIK---------------KFLESDDDKMVKKIamREIKLLKQLRHENLVNLLE 68
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglkkereKRLEKEISRDIRTI--REAALSSLLNHPHICRLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 VCKKKKRWYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd14077   81 FLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 rTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQLyhimmclgnliprHQEL 228
Cdd:cd14077  161 -NLYDPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPF-DDENMPAL-------------HAKI 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 229 fnKNPVFagvrlpeikereplerRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14077  226 --KKGKV----------------EYPSyLSSECKSLISRMLVVDPKKRATLEQVLNHPW 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-284 1.79e-28

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 113.99  E-value: 1.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQ-LRHENLVNLLEVCKKKKRWYLVFEFVD---- 84
Cdd:cd14106   16 LGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELcKDCPRVVNLHEVYETRSELILILELAAggel 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS---GVVKLCDFGFARTLAAPGEVYtDY 161
Cdd:cd14106   96 QTLLDEEECLTE----ADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRVIGEGEEIR-EI 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClgNL-IPRhqELFNknpvfagvrl 240
Cdd:cd14106  171 LGTPDYVAPEILSYE-PISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQC--NLdFPE--ELFK---------- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578809600 241 peikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14106  236 --------------DVSPLAIDFIKRLLVKDPEKRLTAKECLEH 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
10-206 1.84e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 115.69  E-value: 1.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM--VKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD--- 84
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMkqVQHV-AQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVgge 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 -HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaaPGEVYTdYVA 163
Cdd:PTZ00263 105 lFTHLRKAGRFPN----DVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV--PDRTFT-LCG 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809600 164 TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:PTZ00263 178 TPEYLAPEVIQSK-GHGKAVDWWTMGVLLYEFIAGYPPFFDDT 219
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
4-284 1.97e-28

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 113.64  E-value: 1.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESD-DDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQlDEENLKKI-YREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLeLFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaAPGEVYTDY 161
Cdd:cd14071   81 ASNGEIFDY-LAQHGrMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFF-KPGELLKTW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVKYGKAVDVWAIGCLvtemfmgeplfpgdsdidqLYhIMMClGNLiPrhqelfnknpvFAGVRLP 241
Cdd:cd14071  159 CGSPPYAAPEVFEGKEYEGPQLDIWSLGVV-------------------LY-VLVC-GAL-P-----------FDGSTLQ 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 242 EIKERePLERRY--PK-LSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14071  206 TLRDR-VLSGRFriPFfMSTDCEHLIRRMLVLDPSKRLTIEQIKKH 250
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
3-204 2.44e-28

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 113.38  E-value: 2.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTilddlELFpnglDYQVVQKYL--------F-QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaA 153
Cdd:cd14072   81 ASGG-----EVF----DYLVAHGRMkekearakFrQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEF-T 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPG 204
Cdd:cd14072  151 PGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG 201
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
3-287 3.37e-28

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 113.10  E-value: 3.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvkkIAMR-------EIKLLKQ---LRHENLVNLLEVCKK 72
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEW---AMINgpvpvplEIALLLKaskPGVPGVIRLLDWYER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  73 KKRWYLVFEFVDHTIldDLELFPNG---LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS-QSGVVKLCDFGFA 148
Cdd:cd14005   78 PDGFLLIMERPEPCQ--DLFDFITErgaLSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 RTLAApgEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEplfpgdsdidqlyhimmclgnlIPRHQEL 228
Cdd:cd14005  156 ALLKD--SVYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGD----------------------IPFENDE 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 229 fnknpvfagvrlpEIKEREPLERryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14005  212 -------------QILRGNVLFR--PRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
10-276 3.39e-28

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 113.37  E-value: 3.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKF--LESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIdkKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELCPGGN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGevYTDYVATRW- 166
Cdd:cd14070   90 LMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILG--YSDPFSTQCg 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 ---YRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDS-DIDQLYHIMMclgnliprhqelfnknpvfagvrlpe 242
Cdd:cd14070  168 spaYAAPELL-ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQKMV-------------------------- 220
                        250       260       270
                 ....*....|....*....|....*....|....
gi 578809600 243 IKEREPLErryPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd14070  221 DKEMNPLP---TDLSPGAISFLRSLLEPDPLKRP 251
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
30-198 3.64e-28

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 112.82  E-value: 3.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  30 VAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTilddlELF----PNGLDYQVVQK 105
Cdd:cd14075   30 VAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG-----ELYtkisTEGKLSESEAK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 106 YLF-QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVD 184
Cdd:cd14075  105 PLFaQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFS-THAKRGETLNTFCGSPPYAAPELFKDEHYIGIYVD 183
                        170
                 ....*....|....
gi 578809600 185 VWAIGCLVTEMFMG 198
Cdd:cd14075  184 IWALGVLLYFMVTG 197
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
3-285 4.42e-28

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 112.80  E-value: 4.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAM--REIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKII---DKAKCKGKEHMieNEVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDlelfpnglDYQVVQKY--------LFQIINGIGFCHSHNIIHRDIKPENILV--SQSGV--VKLCDFGFA 148
Cdd:cd14095   78 ELVKGGDLFD--------AITSSTKFterdasrmVTDLAQALKYLHSLSIVHRDIKPENLLVveHEDGSksLKLADFGLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 RTLAAPgeVYTdYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQlyhimmclgnliprhQEL 228
Cdd:cd14095  150 TEVKEP--LFT-VCGTPTYVAPEIL-AETGYGLKVDIWAAGVITYILLCGFPPFRSPDR-DQ---------------EEL 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 229 FNKnpVFAGvrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd14095  210 FDL--ILAG-------EFEFLSPYWDNISDSAKDLISRMLVVDPEKRYSAGQVLDHP 257
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-284 4.80e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 112.52  E-value: 4.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd08220   81 APGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKrTVVKIGDFGISKILSSKSKAYT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 dYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclGNliprhqelfnknpvFAgvr 239
Cdd:cd08220  161 -VVGTPCYISPELCEGK-PYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMR--GT--------------FA--- 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 240 lpeikerePLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd08220  220 --------PISDRY---SEELRHLILSMLHLDPNKRPTLSEIMAQ 253
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
5-295 5.57e-28

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 113.40  E-value: 5.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd06622    4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFNQIIM-ELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDL---ELFPNGLDYQVVQKYLFQIINGIGFC-HSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgEVYTD 160
Cdd:cd06622   83 AGSLDKLyagGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVA--SLAKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELL-----VGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprhqelfnKNPVF 235
Cdd:cd06622  161 NIGCQSYMAPERIksggpNQNPTYTVQSDVWSLGLSILEMALGRYPYPPET------------------------YANIF 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 236 AgvRLPEIKEREPlERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAER 295
Cdd:cd06622  217 A--QLSAIVDGDP-PTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADV 273
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
11-286 7.29e-28

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 112.00  E-value: 7.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNK-DTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHtilD 89
Cdd:cd14121    4 GSGTYATVYKAYRKsGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSG---G 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNG---LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG--VVKLCDFGFARTLaAPGEVYTDYVAT 164
Cdd:cd14121   81 DLSRFIRSrrtLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHL-KPNDEAHSLRGS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprHQELFNKnpvfagvrlpeIK 244
Cdd:cd14121  160 PLYMAPEMILKK-KYDARVDLWSVGVILYECLFGRAPFASRS------------------FEELEEK-----------IR 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578809600 245 EREPLE-RRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14121  210 SSKPIEiPTRPELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
4-232 8.49e-28

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 112.91  E-value: 8.49e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdddKMVKKIAMREIK-------LLKQLRHENLVNLLEVCKKKKRW 76
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVM------AIPEVIRLKQEQhvhnekrVLKEVSHPFIIRLFWTEHDQRFL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd05612   77 YMLMEYVPggelFSYLRNSGRFSN----STGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 apGEVYTdYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdIDQLYHIMMcLGNL-IPRHQELFNK 231
Cdd:cd05612  153 --DRTWT-LCGTPEYLAPEVI-QSKGHNKAVDWWALGILIYEMLVGYPPFFDDN-PFGIYEKIL-AGKLeFPRHLDLYAK 226

                 .
gi 578809600 232 N 232
Cdd:cd05612  227 D 227
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-217 9.25e-28

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 111.69  E-value: 9.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMvkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd14083    3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKcidkKALKGKEDSL-----ENEIAVLRKIKHPNIVQLLDIYESKSHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTilddlELFPngldyQVVQK--Y--------LFQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCD 144
Cdd:cd14083   78 LVMELVTGG-----ELFD-----RIVEKgsYtekdashlIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISD 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 145 FGFARTLAapGEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC 217
Cdd:cd14083  148 FGLSKMED--SGVMSTACGTPGYVAPEVL-AQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKA 217
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
4-324 9.29e-28

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 113.22  E-value: 9.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVK-KIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd06635   27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGevyTDYV 162
Cdd:cd06635  107 CLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSA-SIASPA---NSFV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVG--DVKYGKAVDVWAIGCLVTEmfmgeplfpgdsdidqlyhimmclgnLIPRHQELFNKNPVFAgvrL 240
Cdd:cd06635  183 GTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIE--------------------------LAERKPPLFNMNAMSA---L 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 241 PEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMdgfaERFSQELQLKVQKDARNVSLSKKSQNR 320
Cdd:cd06635  234 YHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLR----ERPETVLIDLIQRTKDAVRELDNLQYR 309

                 ....
gi 578809600 321 KKEK 324
Cdd:cd06635  310 KMKK 313
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
9-224 1.32e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 111.64  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14202    9 LIGHGAFAVVFKGRHKEKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---------VVKLCDFGFARTLAAPGEVYT 159
Cdd:cd14202   89 ADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARYLQNNMMAAT 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 160 dYVATRWYRAPELLVGDVKYGKAvDVWAIGCLVTEMFMGEPLFPGDS--DIDQLYHIMMCLGNLIPR 224
Cdd:cd14202  169 -LCGSPMYMAPEVIMSQHYDAKA-DLWSIGTIIYQCLTGKAPFQASSpqDLRLFYEKNKSLSPNIPR 233
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
10-217 1.75e-27

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 110.78  E-value: 1.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK--KFLESDDDKMVKkiamREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV---- 83
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKfiKCRKAKDREDVR----NEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVagge 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 --DHTILDDLELFPNgldyqVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL-VSQSG-VVKLCDFGFARTLaAPGEVYT 159
Cdd:cd14103   77 lfERVVDDDFELTER-----DCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGnQIKIIDFGLARKY-DPDKKLK 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 160 DYVATRWYRAPELlvgdVKY---GKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC 217
Cdd:cd14103  151 VLFGTPEFVAPEV----VNYepiSYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA 207
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
10-282 1.82e-27

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 111.00  E-value: 1.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVM--KCRNKDTGRIVAIKKFLESDDDkmvkkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-T 86
Cdd:cd05059   12 LGSGQFGVVHlgKWRGKIDVAIKMIKEGSMSEDD------FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANgC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRW 166
Cdd:cd05059   86 LLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVL--DDEYTSSVGTKF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 ---YRAPELLVGDvKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYHIMMclgnliprhqelfnknpvfaGVRLPE 242
Cdd:cd05059  164 pvkWSPPEVFMYS-KFSSKSDVWSFGVLMWEVFsEGKMPYERFSNSEVVEHISQ--------------------GYRLYR 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 578809600 243 ikereplerryPKL-SEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd05059  223 -----------PHLaPTEVYTIMYSCWHEKPEERPTFKILL 252
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
4-284 1.99e-27

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 110.94  E-value: 1.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd08530    2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVnLGSLSQKE-REDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDhtiLDDL-----------ELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTL 151
Cdd:cd08530   81 AP---FGDLskliskrkkkrRLFPE----DDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS-KV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPGEVYTDyVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnliprHQELFNK 231
Cdd:cd08530  153 LKKNLAKTQ-IGTPLYAAPEVW-KGRPYDYKSDIWSLGCLLYEMATFRPPFEART------------------MQELRYK 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 232 npVFAGvRLPEIKereplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd08530  213 --VCRG-KFPPIP---------PVYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
5-294 2.01e-27

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 112.00  E-value: 2.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKK-IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd06659   24 ENYVKIGEGSTGVVCIAREKHSGRQVAVKMM---DLRKQQRReLLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVA 163
Cdd:cd06659  101 QGGALTDI-VSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlyhimmclgnliprhqelFNKNPVFAGVRLPEi 243
Cdd:cd06659  180 TPYWMAPE-VISRCPYGTEVDIWSLGIMVIEMVDGEPPY--------------------------FSDSPVQAMKRLRD- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 244 kEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAE 294
Cdd:cd06659  232 -SPPPKLKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPE 281
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
10-227 2.02e-27

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 110.72  E-value: 2.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDdkMVKKIAMREIKLLKQLRHENLVNLLEVCK-KKKRWYLVFEFVDH 85
Cdd:cd14164    8 IGEGSFSKVKLATSQKYCCKVAIKivdRRRASPD--FVQKFLPRELSILRRVNHPNIVQMFECIEvANGRLYIVMEAAAT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLElfPNGLDYQVVQKYLF-QIINGIGFCHSHNIIHRDIKPENILVSQSG-VVKLCDFGFARTLAAPGEVYTDYVA 163
Cdd:cd14164   86 DLLQKIQ--EVHHIPKDLARDMFaQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELSTTFCG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 164 TRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGepLFPGDSDIDQLyhimmclgnliPRHQE 227
Cdd:cd14164  164 SRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTG--TMPFDETNVRR-----------LRLQQ 214
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
6-281 2.86e-27

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 111.32  E-value: 2.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   6 NLGLVGEGSYGMVMKCR----NKDTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW--YLV 79
Cdd:cd05038    8 FIKQLGEGHFGSVELCRydplGDNTGEQVAVKS-LQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRRslRLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd05038   87 MEYLPSGSLRDyLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEYY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 T----DYVATRWYrAPELLvGDVKYGKAVDVWAIGCLVTEMF-MGEPlfpgDSDIDQLYHIMMCLGNLIPRHQELFN--K 231
Cdd:cd05038  167 YvkepGESPIFWY-APECL-RESRFSSASDVWSFGVTLYELFtYGDP----SQSPPALFLRMIGIAQGQMIVTRLLEllK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 232 NpvfaGVRLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd05038  241 S----GERLP----------RPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
4-311 3.25e-27

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 111.19  E-value: 3.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesddDKmVKKIAMREIK-LLKQLRHENLVNLLEVCKKKKRWYLVFEf 82
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKII-----DK-SKRDPSEEIEiLLRYGQHPNIITLRDVYDDGNSVYLVTE- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 vdhtILDDLELfpngLDYQVVQKYL---------FQIINGIGFCHSHNIIHRDIKPENIL-VSQSG---VVKLCDFGFAR 149
Cdd:cd14091   75 ----LLRGGEL----LDRILRQKFFsereasavmKTLTKTVEYLHSQGVVHRDLKPSNILyADESGdpeSLRICDFGFAK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAP-GEVYTD-YVATrwYRAPELLvgdvK---YGKAVDVWAIGCLVTEMFMGEPLF---PGDSDIDQLYHI---MMCL 218
Cdd:cd14091  147 QLRAEnGLLMTPcYTAN--FVAPEVL----KkqgYDAACDIWSLGVLLYTMLAGYTPFasgPNDTPEVILARIgsgKIDL 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 219 GnliprhqelfnkNPVFAGVrlpeikereplerrypklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQmdgFAERFSQ 298
Cdd:cd14091  221 S------------GGNWDHV------------------SDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR---NRDSLPQ 267
                        330
                 ....*....|...
gi 578809600 299 ElQLKVQKDARNV 311
Cdd:cd14091  268 R-QLTDPQDAALV 279
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1-217 3.42e-27

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 110.37  E-value: 3.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14114    1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESD--KETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFvdhtiLDDLELFP------NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS--QSGVVKLCDFGFARTLa 152
Cdd:cd14114   79 EF-----LSGGELFEriaaehYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHL- 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC 217
Cdd:cd14114  153 DPKESVKVTTGTAEFAAPEIVERE-PVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSC 216
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
9-289 3.42e-27

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 110.56  E-value: 3.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIAMRE--IKLLKQLRHENLVNLLEVCKKKKRWYLVFeFVDH 85
Cdd:cd06651   14 LLGQGAFGRVYLCYDVDTGRELAAKQVqFDPESPETSKEVSALEceIQLLKNLQHERIVQYYGCLRDRAEKTLTI-FMEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 ----TILDDLELFpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---TLAAPGEVY 158
Cdd:cd06651   93 mpggSVKDQLKAY-GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlqTICMSGTGI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGN-LIPRHqelfnknpvfag 237
Cdd:cd06651  172 RSVTGTPYWMSPEVISGE-GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNpQLPSH------------ 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 238 vrlpeikereplerrypkLSEVVIDLAkKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06651  239 ------------------ISEHARDFL-GCIFVEARHRPSAEELLRHPFAQL 271
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-286 3.48e-27

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 110.22  E-value: 3.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW-YLVFEF 82
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDGFlYIVMGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VD----HTILDDLELFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd08223   82 CEggdlYTRLKEQKGVL--LEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqeLFNKNPvfagv 238
Cdd:cd08223  160 TTLIGTPYYMSPELF-SNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKI-------------LEGKLP----- 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 239 rlpeikerePLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd08223  221 ---------PMPKQY---SPELGELIKAMLHQDPEKRPSVKRILRQPY 256
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
10-276 5.00e-27

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 109.83  E-value: 5.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDtgRIVAIKKFlESDDDKmvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD----H 85
Cdd:cd14058    1 VGRGSFGVVCKARWRN--QIVAVKII-ESESEK---KAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEggslY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLELFPnglDYQVVQ--KYLFQIINGIGFCHSHN---IIHRDIKPENILVSQSG-VVKLCDFGFARTLAApgeVYT 159
Cdd:cd14058   75 NVLHGKEPKP---IYTAAHamSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGtVLKICDFGTACDIST---HMT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIDqlyhimmclgnliprhqelfnkNPVFAGVR 239
Cdd:cd14058  149 NNKGSAAWMAPEVFEGS-KYSEKCDVFSWGIILWEVITRRKPF---DHIG----------------------GPAFRIMW 202
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 578809600 240 LPEIKEREPLERRYPKLSEvviDLAKKCLHIDPDKRP 276
Cdd:cd14058  203 AVHNGERPPLIKNCPKPIE---SLMTRCWSKDPEKRP 236
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-195 6.14e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 109.52  E-value: 6.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd08218    1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd08218   81 CDGGDLYKRINAQRGVLFPEDQilDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELART 160
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 578809600 161 YVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEM 195
Cdd:cd08218  161 CIGTPYYLSPE-ICENKPYNNKSDIWALGCVLYEM 194
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
3-224 7.48e-27

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 109.71  E-value: 7.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRN-KDTGRIVAIKKFLESDDDKMvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14201    7 EYSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKS-QILLGKEIKILKELQHENIVALYDVQEMPNSVFLVME 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ--------SGV-VKLCDFGFARTLA 152
Cdd:cd14201   86 YCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYasrkkssvSGIrIKIADFGFARYLQ 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 153 APGEVYTdYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDS--DIDQLYHIMMCLGNLIPR 224
Cdd:cd14201  166 SNMMAAT-LCGSPMYMAPEVIMSQ-HYDAKADLWSIGTVIYQCLVGKPPFQANSpqDLRMFYEKNKNLQPSIPR 237
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
10-216 8.35e-27

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 109.50  E-value: 8.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMV-----MKCRNKDTGRIVAIKKFLES---DDDKMVKkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14076    9 LGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDtqqENCQTSK--IMREINILKGLTHPNIVRLLDVLKTKKYIGIVLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL-AAPGEVYTD 160
Cdd:cd14076   87 FVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdHFNGDLMST 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 161 YVATRWYRAPELLVGDVKY-GKAVDVWAIGCLVTEMFMG------EPLFPGDSDIDQLYHIMM 216
Cdd:cd14076  167 SCGSPCYAAPELVVSDSMYaGRKADIWSCGVILYAMLAGylpfddDPHNPNGDNVPRLYRYIC 229
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
10-287 1.05e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 108.67  E-value: 1.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd08221    8 LGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DL------ELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVA 163
Cdd:cd08221   88 DKiaqqknQLFPE----EVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfnknpvfagvrlpei 243
Cdd:cd08221  164 TPYYMSPELVQGV-KYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ--------------------------- 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578809600 244 KEREPLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd08221  216 GEYEDIDEQY---SEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-233 1.25e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 108.52  E-value: 1.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVED-SRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VD-----HTILDDL-ELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd08219   80 CDggdlmQKIKLQRgKLFPE----DTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmCLG--NLIPRH--------- 225
Cdd:cd08219  156 YACTYVGTPYYVPPEIW-ENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKV--CQGsyKPLPSHysyelrsli 232

                 ....*...
gi 578809600 226 QELFNKNP 233
Cdd:cd08219  233 KQMFKRNP 240
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
2-212 1.85e-26

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 109.03  E-value: 1.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVK----KIAMREIKLLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIL---DKQKVVKlkqvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVdhtilddlelfPNGLDYQVVQK-----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd14209   78 MVMEYV-----------PGGEMFSHLRRigrfsepharfYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFG 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 147 FARTLAapGEVYTdYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIdQLY 212
Cdd:cd14209  147 FAKRVK--GRTWT-LCGTPEYLAPEIILSK-GYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIY 207
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
4-288 1.99e-26

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 109.34  E-value: 1.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVK-KIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKwQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGevyTDYV 162
Cdd:cd06634   97 CLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA-SIMAPA---NSFV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVG--DVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnliprhqelfNKNPVFagvrl 240
Cdd:cd06634  173 GTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQ-------------NESPAL----- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 241 peikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06634  235 -----------QSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLL 271
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2-284 2.20e-26

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 109.06  E-value: 2.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCR-NKDTGRIVAIK---KFLESDDDKMVKKIA--MREIKLLKQLRHENLVNLLEVCKKKKR 75
Cdd:cd14096    1 ENYRLINKIGEGAFSNVYKAVpLRNTGKPVAIKvvrKADLSSDNLKGSSRAniLKEVQIMKRLSHPNIVKLLDFQESDEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVD-----HTILDdLELFPNGLDYQVVQkylfQIINGIGFCHSHNIIHRDIKPENILVS-----QS-------- 137
Cdd:cd14096   81 YYIVLELADggeifHQIVR-LTYFSEDLSRHVIT----QVASAVKYLHEIGVVHRDIKPENLLFEpipfiPSivklrkad 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 138 --------------------GVVKLCDFGFARTLaAPGEVYTDyVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFM 197
Cdd:cd14096  156 ddetkvdegefipgvggggiGIVKLADFGLSKQV-WDSNTKTP-CGTVGYTAPE-VVKDERYSKKVDMWALGCVLYTLLC 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 198 GEPLFPgDSDIDQlyhimmcLGNLIPRHQELFnknpvfagvrlpeikerepLERRYPKLSEVVIDLAKKCLHIDPDKRPF 277
Cdd:cd14096  233 GFPPFY-DESIET-------LTEKISRGDYTF-------------------LSPWWDEISKSAKDLISHLLTVDPAKRYD 285

                 ....*..
gi 578809600 278 CAELLHH 284
Cdd:cd14096  286 IDEFLAH 292
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
2-286 2.37e-26

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 108.58  E-value: 2.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGrIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06643    5 DFWEIVGELGDGAFGKVYKAQNKETG-ILAAAKVIDTKSEEELEDY-MVEIDILASCDHPNIVKLLDAFYYENNLWILIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 F-----VDHTILDdLELFPNGLDYQVVQKylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd06643   83 FcaggaVDAVMLE-LERPLTEPQIRVVCK---QTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPlfpgdsdidqlyhimmclgnliPRHQelfnKN 232
Cdd:cd06643  159 RRDSFIGTPYWMAPEVVMcetsKDRPYDYKADVWSLGVTLIEMAQIEP----------------------PHHE----LN 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 233 PVFAgvrLPEIKEREPLERRYP-KLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06643  213 PMRV---LLKIAKSEPPTLAQPsRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPF 264
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
5-286 2.97e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 109.91  E-value: 2.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:PLN00034  77 ERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTVRRQIC-REIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFpnglDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVAT 164
Cdd:PLN00034 156 GGSLEGTHIA----DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTMDPCNSSVGT 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDVKYGK----AVDVWAIGCLVTEMFMGEplFP------GDsdidqlYHIMMClgnliprhqelfnknpv 234
Cdd:PLN00034 232 IAYMSPERINTDLNHGAydgyAGDIWSLGVSILEFYLGR--FPfgvgrqGD------WASLMC----------------- 286
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 235 fagvrlpEIKEREPLERRyPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:PLN00034 287 -------AICMSQPPEAP-ATASREFRHFISCCLQREPAKRWSAMQLLQHPF 330
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-284 3.48e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 107.42  E-value: 3.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKKIAmreikLLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKciakKALEGKETSIENEIA-----VLHKIKHPNIVALDDIYESGGHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL---VSQSGVVKLCDFGFARtLAAP 154
Cdd:cd14167   78 LIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK-IEGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClgnliprhqelfnknpv 234
Cdd:cd14167  157 GSVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKA----------------- 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 235 fagvrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14167  219 ----------EYEFDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQH 258
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
3-204 5.42e-26

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 106.96  E-value: 5.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKdTGRIVAIKKFLES---DDDKMVKkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14161    4 RYEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDrikDEQDLLH--IRREIEIMSSLNHPHIISVYEVFENSSKIVIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArTLAAPGEVYT 159
Cdd:cd14161   81 MEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS-NLYNQDKFLQ 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPG 204
Cdd:cd14161  160 TYCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDG 204
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
7-206 7.66e-26

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 107.88  E-value: 7.66e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCR---NKDTGRIVAIK-----KFLESDDDKMVKKiAMREIklLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd05584    1 LKVLGKGGYGKVFQVRkttGSDKGKIFAMKvlkkaSIVRNQKDTAHTK-AERNI--LEAVKHPFIVDLHYAFQTGGKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd05584   78 ILEYLSggelFMHLEREGIFME----DTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 155 GEVYTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd05584  154 GTVTHTFCGTIEYMAPEILT-RSGHGKAVDWWSLGALMYDMLTGAPPFTAEN 204
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
10-205 1.33e-25

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 105.93  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKdtGRIVAIKKFlesddDKMVKKIAMR-----EIKLLKqLRHENLVNLL--EVCKKKKRWYLV-FE 81
Cdd:cd13979   11 LGSGGFGSVYKATYK--GETVAVKIV-----RRRRKNRASRqsfwaELNAAR-LRHENIVRVLaaETGTDFASLGLIiME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVD----HTILDDLELfPNGLDYQVvqKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV 157
Cdd:cd13979   83 YCGngtlQQLIYEGSE-PLPLAHRI--LISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGNEV 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 158 YTDYV---ATRWYRAPELLVGDVKYGKAvDVWAIGCLVTEMFMGEPLFPGD 205
Cdd:cd13979  160 GTPRShigGTYTYRAPELLKGERVTPKA-DIYSFGITLWQMLTRELPYAGL 209
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
10-286 1.59e-25

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 105.84  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFlesddDKMVKKIAMREIKLLKQLRHENLVNLLEvckkkkrWYlvfEFVDHTILD 89
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKCV-----DKSKRPEVLNEVRLTHELKHPNVLKFYE-------WY---ETSNHLWLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 dLELFPNG-----------LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA------ 152
Cdd:cd14010   73 -VEYCTGGdletllrqdgnLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGeilkel 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 ----------APGEVYTDYVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhimmclgnli 222
Cdd:cd14010  152 fgqfsdegnvNKVSKKQAKRGTPYYMAPELFQGGV-HSFASDLWALGCVLYEMFTGKPPFVAES---------------- 214
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 223 prHQELFNKnpvfagvrlpeIKEREPLE---RRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14010  215 --FTELVEK-----------ILNEDPPPpppKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
10-212 2.11e-25

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 106.63  E-value: 2.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKflesdddkMVKKIAMR--EIK--------LLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKV--------LQKKAILKrnEVKhimaernvLLKNVKHPFLVGLHYSFQTKDKLYFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTilddlELFPNgldyqvVQK-----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd05575   75 LDYVNGG-----ELFFH------LQRerhfpeprarfYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLC 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 149 RTLAAPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLY 212
Cdd:cd05575  144 KEGIEPSDTTSTFCGTPEYLAPEVLRKQ-PYDRTVDWWCLGAVLYEMLYGLPPFY-SRDTAEMY 205
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
10-251 2.88e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 105.51  E-value: 2.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQR--RELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRA 169
Cdd:cd06658  108 DI-VTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 170 PElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclGNLIPRHQELFNKNPVFAGVrLPEIKEREPL 249
Cdd:cd06658  187 PE-VISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIR---DNLPPRVKDSHKVSSVLRGF-LDLMLVREPS 261

                 ..
gi 578809600 250 ER 251
Cdd:cd06658  262 QR 263
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
10-251 3.05e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 105.49  E-value: 3.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQR--RELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRA 169
Cdd:cd06657  106 DI-VTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 170 PElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLyhiMMCLGNLIPRHQELFNKNPVFAGVrLPEIKEREPL 249
Cdd:cd06657  185 PE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAM---KMIRDNLPPKLKNLHKVSPSLKGF-LDRLLVRDPA 259

                 ..
gi 578809600 250 ER 251
Cdd:cd06657  260 QR 261
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
2-221 4.81e-25

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 104.31  E-value: 4.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREYALK-IINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVME 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ----SGVVKLCDFGFARTLAAPgeV 157
Cdd:cd14183   85 LVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLATVVDGP--L 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 158 YTdYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNL 221
Cdd:cd14183  163 YT-VCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQV 224
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
10-286 5.02e-25

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 104.51  E-value: 5.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TIL 88
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEE--AQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGgTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV----------- 157
Cdd:cd14154   79 DVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERLPsgnmspsetlr 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 ----------YTdYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFmgeplfpGDSDIDQLYhimmclgnlIPRHQE 227
Cdd:cd14154  159 hlkspdrkkrYT-VVGNPYWMAPEMLNG-RSYDEKVDIFSFGIVLCEII-------GRVEADPDY---------LPRTKD 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 228 lFNKNpvfagvrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPfCAELLHHDF 286
Cdd:cd14154  221 -FGLN------------VDSFREKFCAGCPPPFFKLAFLCCDLDPEKRP-PFETLEEWL 265
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
4-214 5.12e-25

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 104.49  E-value: 5.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVA---IKKFLESDDDKMVKKIAM-REIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14105    7 YDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRGVSREDIeREVSILRQVLHPNIITLHDVFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV----VKLCDFGFARTLaAPG 155
Cdd:cd14105   87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKI-EDG 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 156 EVYTDYVATRWYRAPELlvgdVKY---GKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd14105  166 NEFKNIFGTPEFVAPEI----VNYeplGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 223
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
8-288 5.71e-25

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 105.07  E-value: 5.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   8 GLVGEGSYGMVMKCRNKDTGRIVAIKKflesdddkMVKKI-AMREIKLLKQLR-HENLVNLLEVCKKKKRWYLVFEFvdh 85
Cdd:cd14092   12 EALGDGSFSVCRKCVHKKTGQEFAVKI--------VSRRLdTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMEL--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 tiLDDLELFPngldyQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARtLA 152
Cdd:cd14092   81 --LRGGELLE-----RIRKKKRFteseasrimrQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFAR-LK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDVK---YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLgnlipRHQElF 229
Cdd:cd14092  153 PENQPLKTPCFTLPYAAPEVLKQALStqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMKRI-----KSGD-F 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 230 NknpvFAGvrlPEIKEreplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14092  227 S----FDG---EEWKN----------VSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQ 268
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
2-221 6.51e-25

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 103.96  E-value: 6.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKK--IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKII---DKAKCCGKehLIENEVSILRRVKHPNIIMLIEEMDTPAELYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ----SGVVKLCDFGFARTLAAPg 155
Cdd:cd14184   78 MELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLATVVEGP- 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 156 eVYTdYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNL 221
Cdd:cd14184  157 -LYT-VCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILLGKL 219
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
7-196 6.78e-25

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 104.33  E-value: 6.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCR----NKDTGRIVAIKKFLESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKR--WYLVF 80
Cdd:cd14205    9 LQQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEHL--RDFEREIEILKSLQHDNIVKYKGVCYSAGRrnLRLIM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd14205   87 EYLPYGSLRDyLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYK 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809600 160 ----DYVATRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF 196
Cdd:cd14205  167 vkepGESPIFWY-APESLT-ESKFSVASDVWSFGVVLYELF 205
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
2-285 7.32e-25

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 103.62  E-value: 7.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDDKMVKkiamREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd14078    3 KYYELHETIGSGGFAKVKLATHILTGEKVAIKimdKKALGDDLPRVK----TEIEALKNLSHQHICRLYHVIETDNKIFM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDhtildDLELFpnglDYQVVQ---------KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAr 149
Cdd:cd14078   79 VLEYCP-----GGELF----DYIVAKdrlsedearVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLC- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 tlAAPGEVYTDYVAT----RWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGepLFPGDSDidqlyhIMMCLGNLIPRH 225
Cdd:cd14078  149 --AKPKGGMDHHLETccgsPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCG--FLPFDDD------NVMALYRKIQSG 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 226 qelfnknpvfagvrlpeiKEREPlerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd14078  219 ------------------KYEEP-----EWLSPSSKLLLDQMLQVDPKKRITVKELLNHP 255
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
9-212 7.99e-25

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 105.05  E-value: 7.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK-----KFLESDDDKMVkkIAMREIkLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05603    2 VIGKGSFGKVLLAKRKCDGKFYAVKvlqkkTILKKKEQNHI--MAERNV-LLKNLKHPFLVGLHYSFQTSEKLYFVLDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTilddlELFpngldYQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd05603   79 NGG-----ELF-----FHLQRErcfleprarfYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGME 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLY 212
Cdd:cd05603  149 PEETTSTFCGTPEYLAPEVLRKE-PYDRTVDWWCLGAVLYEMLYGLPPFY-SRDVSQMY 205
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
10-283 8.76e-25

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 103.29  E-value: 8.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TIL 88
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLKRKF-LQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGgSLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYT-----DYVA 163
Cdd:cd05041   82 TFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEE--DGEYTvsdglKQIP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWyRAPE-LLVGdvKYGKAVDVWAIGCLVTEMF-MGEPLFPGdsdidqlyhimmcLGNLIPRHQelfnknpVFAGVRLP 241
Cdd:cd05041  160 IKW-TAPEaLNYG--RYTSESDVWSFGILLWEIFsLGATPYPG-------------MSNQQTREQ-------IESGYRMP 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578809600 242 EikereplerryPKLS-EVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd05041  217 A-----------PELCpEAVYRLMLQCWAYDPENRPSFSEIYN 248
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
9-212 9.16e-25

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 104.58  E-value: 9.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLES---DDDKMVKKIAMREIklLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAhivSRSEVTHTLAERTV--LAQVDCPFIVPLKFSFQSPEKLYLVLAFING 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TilddlELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd05585   79 G-----ELFhhlqrEGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNT 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 161 YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLY 212
Cdd:cd05585  154 FCGTPEYLAPELLLGH-GYTKAVDWWTLGVLLYEMLTGLPPFY-DENTNEMY 203
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
10-284 9.65e-25

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 103.40  E-value: 9.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLeLFPNGLDYQVVQKYLFQ-IINGIGFCHSHNIIHRDIKPENILVSQSGV-------VKLCDFGFARTLAAPGE-VYTD 160
Cdd:cd14097   89 EL-LLRKGFFSENETRHIIQsLASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSVQKYGLGEdMLQE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQLYHIMmclgnlipRHQELFNKNPVFAGVrl 240
Cdd:cd14097  168 TCGTPIYMAPEVISAH-GYSQQCDIWSIGVIMYMLLCGEPPFVAKSE-EKLFEEI--------RKGDLTFTQSVWQSV-- 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578809600 241 peikereplerrypklSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14097  236 ----------------SDAAKNVLQQLLKVDPAHRMTASELLDN 263
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
2-222 9.83e-25

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 104.62  E-value: 9.83e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKKIAMREIK----LLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSE---MLEKEQVAHVRaerdILAEADNPWVVKLYYSFQDEENLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd05599   78 LIMEFLPggdmMTLLMKKDTLTE----EETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKK 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 154 PGEVYTDyVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMCLGNLI 222
Cdd:cd05599  154 SHLAYST-VGTPDYIAPEVFLQK-GYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRETLV 220
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
4-206 1.01e-24

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 107.96  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGsyGMVMKCRNKDT--GRIVAIKkFLESD---DDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:NF033483   9 YEIGERIGRG--GMAEVYLAKDTrlDRDVAVK-VLRPDlarDPEFVARFR-REAQSAASLSHPNIVSVYDVGEDGGIPYI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDL--ELFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:NF033483  85 VMEYVDGRTLKDYirEHGP--LSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSTTM 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 157 VYTDYV-ATRWYRAPELlvgdVKYGKA---VDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:NF033483 163 TQTNSVlGTVHYLSPEQ----ARGGTVdarSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
2-214 1.06e-24

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 103.56  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVA---IKKFLESDDDKMVKKIAM-REIKLLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAakfIKKRRTKSSRRGVSREDIeREVSILKEIQHPNVITLHEVYENKTDVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV----VKLCDFGFARTLAA 153
Cdd:cd14194   85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKIDF 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 154 pGEVYTDYVATRWYRAPELlvgdVKY---GKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd14194  165 -GNEFKNIFGTPEFVAPEI----VNYeplGLEADMWSIGVITYILLSGASPFLGDTKQETLANV 223
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
10-276 1.13e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 103.57  E-value: 1.13e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKK--FLESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd08228   10 IGRGQFSEVYRATCLLDRKPVALKKvqIFEMMDAK-ARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDL--------ELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd08228   89 LSQMikyfkkqkRLIPE----RTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDsdidqlyhimmclgnliprhqelfnKNPVFAGVR 239
Cdd:cd08228  165 SLVGTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD-------------------------KMNLFSLCQ 218
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 578809600 240 LPEIKEREPLERRYpkLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd08228  219 KIEQCDYPPLPTEH--YSEKLRELVSMCIYPDPDQRP 253
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
10-287 1.51e-24

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 102.69  E-value: 1.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFefvdhtILd 89
Cdd:cd13983    9 LGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIF------IT- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 dlELFPNG-----------LDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILV-SQSGVVKLCDFGFArTLAAPG 155
Cdd:cd13983   82 --ELMTSGtlkqylkrfkrLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFInGNTGEVKIGDLGLA-TLLRQS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTdYVATRWYRAPELLvgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHimMCLGNLIPrhqELFNKnpvf 235
Cdd:cd13983  159 FAKS-VIGTPEFMAPEMY--EEHYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYK--KVTSGIKP---ESLSK---- 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 236 agVRLPEIKereplerrypklsevviDLAKKCLHiDPDKRPFCAELLHHDFF 287
Cdd:cd13983  227 --VKDPELK-----------------DFIEKCLK-PPDERPSARELLEHPFF 258
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
4-276 1.70e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 102.97  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTG-RIVAIKKF---------LESDDDKMVKKIaMREIKLLK-QLRHENLVNLLEVCKK 72
Cdd:cd08528    2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEInmtnpafgrTEQERDKSVGDI-ISEVNIIKeQLRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  73 KKRWYLVFEFVDHTILDDL--------ELFPNGLDYQVVqkylFQIINGIGFCHSHN-IIHRDIKPENILVSQSGVVKLC 143
Cdd:cd08528   81 NDRLYIVMELIEGAPLGEHfsslkeknEHFTEDRIWNIF----VQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTIT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 144 DFGFARTLAAPGEVYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqlyhiMMCLGNLIp 223
Cdd:cd08528  157 DFGLAKQKGPESSKMTSVVGTILYSCPE-IVQNEPYGEKADIWALGCILYQMCTLQPPFYSTN--------MLTLATKI- 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 224 rhqelfnknpVFAgvrlpeikEREPL-ERRYpklSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd08528  227 ----------VEA--------EYEPLpEGMY---SDDITFVIRSCLTPDPEARP 259
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
11-203 2.05e-24

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 103.30  E-value: 2.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKK--FLESDDDKMVKKIAMrEIKLLKQLRHENLVNL------LEVCKKKKRWYLVFEF 82
Cdd:cd13989    2 GSGGFGYVTLWKHQDTGEYVAIKKcrQELSPSDKNRERWCL-EVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLAMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDD-LELFPN--GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLAApGE 156
Cdd:cd13989   81 CSGGDLRKvLNQPENccGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgrvIYKLIDLGYAKELDQ-GS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 157 VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG-EPLFP 203
Cdd:cd13989  160 LCTSFVGTLQYLAPELFESK-KYTCTVDYWSFGTLAFECITGyRPFLP 206
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
2-288 2.21e-24

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 104.29  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKK------IAMREIklLKQLRHENLVNLLEVCKKKKR 75
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSD---MLKReqiahvRAERDI--LADADSPWIVRLHYAFQDEDH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFV---D-HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL 151
Cdd:cd05573   76 LYLVMEYMpggDlMNLLIKYDVFPE----ETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKM 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPGEVYTDY-----------------------------VATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05573  152 NKSGDRESYLndsvntlfqdnvlarrrphkqrrvraysaVGTPDYIAPEVLRG-TGYGPECDWWSLGVILYEMLYGFPPF 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 203 PGDSDIDQLYHIMmclgnlipRHQELFnknpvfagvRLPeikereplerRYPKLSEVVIDLAKKCLhIDPDKRpFC--AE 280
Cdd:cd05573  231 YSDSLVETYSKIM--------NWKESL---------VFP----------DDPDVSPEAIDLIRRLL-CDPEDR-LGsaEE 281

                 ....*...
gi 578809600 281 LLHHDFFQ 288
Cdd:cd05573  282 IKAHPFFK 289
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
4-284 2.42e-24

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 102.76  E-value: 2.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRW-----YL 78
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDV--KEAMREIENYRLFNHPNILRLLDSQIVKEAGgkkevYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDH-TILDDLEL-------FPngldyqvvQKYLFQIINGIgfC------HSHNII---HRDIKPENILVSQSGVVK 141
Cdd:cd13986   80 LLPYYKRgSLQDEIERrlvkgtfFP--------EDRILHIFLGI--CrglkamHEPELVpyaHRDIKPGNVLLSEDDEPI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 142 LCDFGFARTlaAPGEVYTDYVATRW-----------YRAPELLvgDVKYG----KAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd13986  150 LMDLGSMNP--ARIEIEGRREALALqdwaaehctmpYRAPELF--DVKSHctidEKTDIWSLGCTLYALMYGESPFERIF 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 207 DIDQLYHIMMCLGNLIPrhqelfnknpvfagvrlpeikerePLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd13986  226 QKGDSLALAVLSGNYSF------------------------PDNSRY---SEELHQLVKSMLVVNPAERPSIDDLLSR 276
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
45-286 2.94e-24

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 101.67  E-value: 2.94e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  45 KKIAMREIKL--LKQLRHENLVNLLEVCKKKK------RWYLVFEFVDHTILDDLeLFPNG-LDYQVVQKYLFQIINGIG 115
Cdd:cd14012   40 KQIQLLEKELesLKKLRHPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSEL-LDSVGsVPLDTARRWTLQLLEALE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 116 FCHSHNIIHRDIKPENILVSQS---GVVKLCDFGFARTLA-APGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCL 191
Cdd:cd14012  119 YLHRNGVVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLLdMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWDLGLL 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 192 VTEMFMGeplfpgdsdidqlyhimmclgnliprhQELFNKNPVFAGVRLPeikereplerryPKLSEVVIDLAKKCLHID 271
Cdd:cd14012  199 FLQMLFG---------------------------LDVLEKYTSPNPVLVS------------LDLSASLQDFLSKCLSLD 239
                        250
                 ....*....|....*
gi 578809600 272 PDKRPFCAELLHHDF 286
Cdd:cd14012  240 PKKRPTALELLPHEF 254
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
3-223 3.29e-24

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 101.96  E-value: 3.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVV-KLCDFGFARTLAAPGEVYT 159
Cdd:cd08225   81 CDGGDLMKRINRQRGVLFSEDQilSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMELAY 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 160 DYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSdidqLYHIMM--CLGNLIP 223
Cdd:cd08225  161 TCVGTPYYLSPE-ICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNN----LHQLVLkiCQGYFAP 221
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
4-286 3.59e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 102.03  E-value: 3.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIK--KFLESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKiiKLEPGDDFSLIQQ----EIFMVKECKHCNIVAYFGSYLSREKLWICME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd06646   87 YCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRKSF 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLVGDVK--YGKAVDVWAIGCLVTEmfmgeplfpgdsdidqlyhimmcLGNLIPrhqELFNKNPVFAGVR 239
Cdd:cd06646  167 IGTPYWMAPEVAAVEKNggYNQLCDIWAVGITAIE-----------------------LAELQP---PMFDLHPMRALFL 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 240 LPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06646  221 MSKSNFQPPKLKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLTHLF 267
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-287 3.84e-24

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 101.50  E-value: 3.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCA-AKFIPLRSS--TRARAFQERDILARLSHRRLTCLLDQFETRKTLILILELC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDlELFPNGLDYQV-VQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV--VKLCDFGFARTLAAPGEVYTD 160
Cdd:cd14107   81 SSEELLD-RLFLKGVVTEAeVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQEITPSEHQFSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YvATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnliprHQELFNKNPVFAgvrl 240
Cdd:cd14107  160 Y-GSPEFVAPE-IVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVA---------EGVVSWDTPEIT---- 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 241 peikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14107  225 --------------HLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
10-214 6.10e-24

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 101.13  E-value: 6.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14108   10 IGRGAFSYLRRVKEKSSDLSFA-AKFIPVRAKK--KTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVTELCHEELLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVvQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV--VKLCDFGFARTLAAPGEVYTDYvATRWY 167
Cdd:cd14108   87 RITKRPTVCESEV-RSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTdqVRICDFGNAQELTPNEPQYCKY-GTPEF 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 168 RAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd14108  165 VAPE-IVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
2-300 6.88e-24

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 101.30  E-value: 6.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06641    4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIdLEEAEDEI--EDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDH-TILDDLElfPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd06641   82 EYLGGgSALDLLE--PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPlfPGDSdidqlYHIMMCLgNLIPRhqelfNKNPVFAGVR 239
Cdd:cd06641  160 *FVGTPFWMAPE-VIKQSAYDSKADIWSLGITAIELARGEP--PHSE-----LHPMKVL-FLIPK-----NNPPTLEGNY 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 240 LPEIKEreplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAERFSQEL 300
Cdd:cd06641  226 SKPLKE-----------------FVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTEL 269
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
11-202 7.69e-24

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 100.83  E-value: 7.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKFLESDDdkmvkkiAMREIKL-LKQLRHENLVNLLEV----CKKKKRWYLVFEFvdh 85
Cdd:cd14089   10 GLGINGKVLECFHKKTGEKFALKVLRDNPK-------ARREVELhWRASGCPHIVRIIDVyentYQGRKCLLVVMEC--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 tiLDDLELFpNGLDYQVVQKY--------LFQIINGIGFCHSHNIIHRDIKPENILVSQ---SGVVKLCDFGFAR----- 149
Cdd:cd14089   80 --MEGGELF-SRIQERADSAFtereaaeiMRQIGSAVAHLHSMNIAHRDLKPENLLYSSkgpNAILKLTDFGFAKetttk 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 150 -TLAAPgeVYTDYvatrwYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14089  157 kSLQTP--CYTPY-----YVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGYPPF 202
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
10-244 7.98e-24

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 101.20  E-value: 7.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKflesdddkMVKKIAMR--------------------------------EIKLLKQ 57
Cdd:cd14199   10 IGKGSYGVVKLAYNEDDNTYYAMKV--------LSKKKLMRqagfprrppprgaraapegctqprgpiervyqEIAILKK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  58 LRHENLVNLLEVCK--KKKRWYLVFEFVDH-TILDDLELFPNGLDYQvvqKYLFQ-IINGIGFCHSHNIIHRDIKPENIL 133
Cdd:cd14199   82 LDHPNVVKLVEVLDdpSEDHLYMVFELVKQgPVMEVPTLKPLSEDQA---RFYFQdLIKGIEYLHYQKIIHRDVKPSNLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 134 VSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKY--GKAVDVWAIG----CLVTEM--FMGE------ 199
Cdd:cd14199  159 VGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIfsGKALDVWAMGvtlyCFVFGQcpFMDErilslh 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 200 ------PL-FPGDSDIDQLyhimmcLGNLIPRhqeLFNKNPVfAGVRLPEIK 244
Cdd:cd14199  239 skiktqPLeFPDQPDISDD------LKDLLFR---MLDKNPE-SRISVPEIK 280
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
10-297 8.02e-24

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 101.11  E-value: 8.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd06619    9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQI-MSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSLD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRWYRA 169
Cdd:cd06619   88 VYRKIPE----HVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV--NSIAKTYVGTNAYMA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 170 PELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPgdsdidqlyHIMMCLGNLIPRH--QELFNKNPvfagVRLPEikere 247
Cdd:cd06619  162 PERISGE-QYGIHSDVWSLGISFMELALGRFPYP---------QIQKNQGSLMPLQllQCIVDEDP----PVLPV----- 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 248 plerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM--DGFAERFS 297
Cdd:cd06619  223 ------GQFSEKFVHFITQCMRKQPKERPAPENLMDHPFIVQynDGNAEVVS 268
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
10-224 8.76e-24

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 100.52  E-value: 8.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKD-TGRIVAIKKFLESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSK-SQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---------VVKLCDFGFARTLaaPGEVYT 159
Cdd:cd14120   80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFL--QDGMMA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 160 dyvATR----WYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDS--DIDQLYHIMMCLGNLIPR 224
Cdd:cd14120  158 ---ATLcgspMYMAPEVIMS-LQYDAKADLWSIGTIVYQCLTGKAPFQAQTpqELKAFYEKNANLRPNIPS 224
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
2-233 9.81e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 100.32  E-value: 9.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKKIAM-----REIKLLKQLRHENLVNLLEVCKKKKRW 76
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMI----DKKAMQKAGMvqrvrNEVEIHCQLKHPSILELYNYFEDSNYV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPG 155
Cdd:cd14186   77 YLVLEMCHNGEMSRyLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClGNLIPRH---------Q 226
Cdd:cd14186  157 EKHFTMCGTPNYISPE-IATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLA-DYEMPAFlsreaqdliH 234

                 ....*..
gi 578809600 227 ELFNKNP 233
Cdd:cd14186  235 QLLRKNP 241
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
3-285 1.06e-23

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 100.96  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNK-DTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLR---HENLVNLLEVCKKKKRWYL 78
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDhtiLDDLELF------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd14052   81 QTELCE---NGSLDVFlselglLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APG--EVYTDyvatRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFM-------GEP---LFPGD-SDIDQLYhimmclg 219
Cdd:cd14052  158 LIRgiEREGD----REYIAPEIL-SEHMYDKPADIFSLGLILLEAAAnvvlpdnGDAwqkLRSGDlSDAPRLS------- 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 220 NLIPRHQELFNKNPvfagvrlpeikerEPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd14052  226 STDLHSASSPSSNP-------------PPDPPNMPILSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
10-284 1.15e-23

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 101.00  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLEsdddkmvKKIAMREIKLLKQLR-HENLVNLLEVCKK----------KKRWYL 78
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKILLD-------RPKARTEVRLHMMCSgHPNIVQIYDVYANsvqfpgesspRARLLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFARTlaAPG 155
Cdd:cd14171   87 VMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAKV--DQG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDYVaTRWYRAPELL----------VGDVK------YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclg 219
Cdd:cd14171  165 DLMTPQF-TPYYVAPQVLeaqrrhrkerSGIPTsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITKDM---- 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 220 nliprhqelfnKNPVFAGvrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14171  240 -----------KRKIMTG-------SYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHH 286
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-288 1.20e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 101.49  E-value: 1.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFlesddDKMVKKIAMREIKLLKQLR-HENLVNLLEVCKKKKRWYLVFEFVDH-TI 87
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKII-----SRRMEANTQREVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRGgEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDL---ELFPNGLDYQVVQkylfQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd14180   89 LDRIkkkARFSESEASQLMR----SLVSAVSFMHEAGVVHRDLKPENILYADESdgaVLKVIDFGFARLRPQGSRPLQTP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHimmclgnliprhqelfnknpvfAGVRLP 241
Cdd:cd14180  165 CFTLQYAAPELF-SNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNH----------------------AADIMH 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 242 EIKE-REPLE-RRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14180  222 KIKEgDFSLEgEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQ 270
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
10-214 1.23e-23

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 100.42  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIAMR-----EIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd14196   13 LGSGQFAIVKKCREKSTGLEYA-AKFIKKRQSRASRRGVSReeierEVSILRQVLHPNIITLHDVYENRTDVVLILELVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV----VKLCDFGFARTLaAPGEVYTD 160
Cdd:cd14196   92 GGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEI-EDGVEFKN 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 161 YVATRWYRAPELlvgdVKY---GKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd14196  171 IFGTPEFVAPEI----VNYeplGLEADMWSIGVITYILLSGASPFLGDTKQETLANI 223
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
10-283 1.23e-23

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 100.66  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvKKIAMREIKLLKQLR-HENLVNLL--------EVCKKKKRWYLVF 80
Cdd:cd14036    8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEK--NKAIIQEINFMKKLSgHPNIVQFCsaasigkeESDQGQAEYLLLT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELF--PNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFARTLAapge 156
Cdd:cd14036   86 ELCKGQLVDFVKKVeaPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEA---- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDY----------------VATRWYRAPEL--LVGDVKYGKAVDVWAIGCLvtemfmgeplfpgdsdidqLYhiMMCl 218
Cdd:cd14036  162 HYPDYswsaqkrslvedeitrNTTPMYRTPEMidLYSNYPIGEKQDIWALGCI-------------------LY--LLC- 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 219 gnliprhqelFNKNPVFAGVRLPEIKER---EPLERRYpklsEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd14036  220 ----------FRKHPFEDGAKLRIINAKytiPPNDTQY----TVFHDLIRSTLKVNPEERLSITEIVE 273
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-288 1.24e-23

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 101.67  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMA-RKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFC-HSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTD 160
Cdd:cd06650   84 HMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGE-PLFPGDSDIDQLyhIMMCLGNLIPRHQELFNKNPVFAGVR 239
Cdd:cd06650  162 FVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVEMAVGRyPIPPPDAKELEL--MFGCQVEGDAAETPPRPRTPGRPLSS 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 240 LPeIKEREPL----------ERRYPKLSEVVI-----DLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06650  239 YG-MDSRPPMaifelldyivNEPPPKLPSGVFslefqDFVNKCLIKNPAERADLKQLMVHAFIK 301
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
10-314 1.32e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 100.87  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDkmvkkiAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14175    9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRD------PSEEIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL-VSQSG---VVKLCDFGFARTLAAPGEVYTDYVAT 164
Cdd:cd14175   83 LDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGnpeSLRICDFGFAKQLRAENGLLMTPCYT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG-EPLFPGDSDIDQlyHIMMCLGNliprhqelfNKNPVFAGvrlpei 243
Cdd:cd14175  163 ANFVAPEVLKRQ-GYDEGCDIWSLGILLYTMLAGyTPFANGPSDTPE--EILTRIGS---------GKFTLSGG------ 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 244 kereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF-QMDGFAERFSQELQLKVQKDARNVSLS 314
Cdd:cd14175  225 --------NWNTVSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWItQKDKLPQSQLNHQDVQLVKGAMAATYS 288
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
9-204 1.38e-23

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 100.57  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKkflesdddkMVKKIA-------MREIKLLKQLR-HENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14090    9 LLGEGAYASVQTCINLYTGKEYAVK---------IIEKHPghsrsrvFREVETLHQCQgHPNILQLIEYFEDDERFYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDH-TILDDLE---LFPNGLDYQVVQkylfQIINGIGFCHSHNIIHRDIKPENILVSQSGV---VKLCDFGFA----- 148
Cdd:cd14090   80 EKMRGgPLLSHIEkrvHFTEQEASLVVR----DIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGsgikl 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 149 -----RTLAAPgEVYTDyVATRWYRAPELL---VGDV-KYGKAVDVWAIGCLVTEMFMGEPLFPG 204
Cdd:cd14090  156 sstsmTPVTTP-ELLTP-VGSAEYMAPEVVdafVGEAlSYDKRCDLWSLGVILYIMLCGYPPFYG 218
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
2-286 1.40e-23

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 100.10  E-value: 1.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRK-VRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL----VSQSGVVkLCDFGFARTlaaPGEV 157
Cdd:cd14088   80 LATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyynrLKNSKIV-ISDFHLAKL---ENGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTDYVATRWYRAPELlVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHimmclgnlipRHQELFNKnpVFAG 237
Cdd:cd14088  156 IKEPCGTPEYLAPEV-VGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEN----------HDKNLFRK--ILAG 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 238 vrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14088  223 -------DYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEW 264
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
10-289 1.42e-23

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 100.19  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLEsddDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TIL 88
Cdd:cd05052   14 LGGGQYGEVYEGVWKKYNLTVAVKTLKE---DTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYgNLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDL------ELFPNGLDYQVVQkylfqIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYV 162
Cdd:cd05052   91 DYLrecnreELNAVVLLYMATQ-----IASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT--GDTYTAHA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRW---YRAPELLVGDvKYGKAVDVWAIGCLVTEMFM-GEPLFPGdSDIDQLYHIMMclgnliprhqelfnknpvfAGV 238
Cdd:cd05052  164 GAKFpikWTAPESLAYN-KFSIKSDVWAFGVLLWEIATyGMSPYPG-IDLSQVYELLE-------------------KGY 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 239 RLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAElLHHDFFQM 289
Cdd:cd05052  223 RME----------RPEGCPPKVYELMRACWQWNPSDRPSFAE-IHQALETM 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
9-284 1.52e-23

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 100.45  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK--KFLESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14166   10 VLGSGAFSEVYLVKQRSTGKLYALKciKKSPLSRDSSLEN----EIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ilddlELFPNGLDYQV-----VQKYLFQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFARtLAAPGeVY 158
Cdd:cd14166   86 -----ELFDRILERGVytekdASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK-MEQNG-IM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPlfpgdsdidqlyhimmclgnliPRHQElfNKNPVFAGV 238
Cdd:cd14166  159 STACGTPGYVAPEVL-AQKPYSKAVDCWSIGVITYILLCGYP----------------------PFYEE--TESRLFEKI 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 239 RLPEIKEREPLerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14166  214 KEGYYEFESPF---WDDISESAKDFIRHLLEKNPSKRYTCEKALSH 256
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
9-287 1.82e-23

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 101.28  E-value: 1.82e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKkflesdddkMVKK---IAMREI-------KLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd05571    2 VLGKGTFGKVILCREKATGELYAIK---------ILKKeviIAKDEVahtltenRVLQNTRHPFLTSLKYSFQTNDRLCF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTilddlELFpngldYQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd05571   73 VMEYVNGG-----ELF-----FHLSRERVFsedrtrfygaEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLC 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 RTLAAPGEVYTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGE-PLFPGDsdidqlyhimmclgnliprHQE 227
Cdd:cd05571  143 KEEISYGATTKTFCGTPEYLAPEVLE-DNDYGRAVDWWGLGVVMYEMMCGRlPFYNRD-------------------HEV 202
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 228 LFnknpvfagvrlpEIKEREPLerRYPK-LSEVVIDLAKKCLHIDPDKR----PFCA-ELLHHDFF 287
Cdd:cd05571  203 LF------------ELILMEEV--RFPStLSPEAKSLLAGLLKKDPKKRlgggPRDAkEIMEHPFF 254
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
7-310 1.89e-23

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 100.93  E-value: 1.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKKIAMREIKLlkQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd05587    1 LMVLGKGSFGKVMLAERKGTDELYAIKilkkDVIIQDDDVECTMVEKRVLAL--SGKPPFLTQLHSCFQTMDRLYFVMEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VdhtilddlelfpNGLD--YQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd05587   79 V------------NGGDlmYHIQQVgkfkepvavfYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhQELFN 230
Cdd:cd05587  147 GIFGGKTTRTFCGTPDYIAPE-IIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDE------------------DELFQ 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 231 knpvfagvrlpEIKEREPlerRYPK-LSEVVIDLAKKCLHIDPDKRPFC-----AELLHHDFFQMDGFAERFSQELQ--- 301
Cdd:cd05587  208 -----------SIMEHNV---SYPKsLSKEAVSICKGLLTKHPAKRLGCgptgeRDIKEHPFFRRIDWEKLERREIQppf 273
                        330
                 ....*....|..
gi 578809600 302 ---LKVQKDARN 310
Cdd:cd05587  274 kpkIKSPRDAEN 285
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
11-286 2.09e-23

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 99.28  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMV-MKCRNKDTgrIVAIKKFLESdddKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TIL 88
Cdd:cd05034    4 GAGQFGEVwMGVWNGTT--KVAVKTLKPG---TMSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKgSLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLE-------LFPNGLDYQVvqkylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgEVYTDY 161
Cdd:cd05034   79 DYLRtgegralRLPQLIDMAA------QIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIED--DEYTAR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRW---YRAPELlvgdVKYGK---AVDVWAIGCLVTEMFM-GEPLFPGdsdidqlyhimmclgnlIPRHQELfnkNPV 234
Cdd:cd05034  151 EGAKFpikWTAPEA----ALYGRftiKSDVWSFGILLYEIVTyGRVPYPG-----------------MTNREVL---EQV 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 235 FAGVRLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRP-FcaELLHHDF 286
Cdd:cd05034  207 ERGYRMP----------KPPGCPDELYDIMLQCWKKEPEERPtF--EYLQSFL 247
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
4-286 2.22e-23

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 100.08  E-value: 2.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIamrEIKLLKQL-RHENLVNLLEVCKKKK------RW 76
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKL---EINMLKKYsHHRNIATYYGAFIKKSppghddQL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDDL--ELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAP 154
Cdd:cd06636   95 WLVMEFCGAGSVTDLvkNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIdqlyHIMMCLgNLIPRhqelfn 230
Cdd:cd06636  175 VGRRNTFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAPPL---CDM----HPMRAL-FLIPR------ 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 231 kNPVfagvrlPEIKEReplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06636  241 -NPP------PKLKSK--------KWSKKFIDFIEGCLVKNYLSRPSTEQLLKHPF 281
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
7-256 2.33e-23

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 100.81  E-value: 2.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESD---DDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVK-VLQKKvilNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 D------HtiLDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEV 157
Cdd:cd05604   80 NggelffH--LQRERSFPE----PRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLYHIMMclgnliprHQELfNKNPvfaG 237
Cdd:cd05604  154 TTTFCGTPEYLAPEVIRKQ-PYDNTVDWWCLGSVLYEMLYGLPPFY-CRDTAEMYENIL--------HKPL-VLRP---G 219
                        250
                 ....*....|....*....
gi 578809600 238 VRLPEIKEREPLERRYPKL 256
Cdd:cd05604  220 ISLTAWSILEELLEKDRQL 238
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
10-202 2.92e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 99.52  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKL----DKKRIKKkkgetMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HtilDDLELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApGEVYT 159
Cdd:cd05577   77 G---GDLKYHiynvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKG-GKKIK 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05577  153 GRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPF 195
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
9-217 3.02e-23

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 99.27  E-value: 3.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTG-----RIVAIKKFLESDDDKmvkkiamREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd14192   11 VLGGGRFGQVHKCTELSTGltlaaKIIKVKGAKEREEVK-------NEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTilddlELFPNGLD--YQVVQ--KYLF--QIINGIGFCHSHNIIHRDIKPENIL-VSQSG-VVKLCDFGFARTLaAPG 155
Cdd:cd14192   84 DGG-----ELFDRITDesYQLTEldAILFtrQICEGVHYLHQHYILHLDLKPENILcVNSTGnQIKIIDFGLARRY-KPR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 156 EVYTDYVATRWYRAPELLVGD-VKYgkAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC 217
Cdd:cd14192  158 EKLKVNFGTPEFLAPEVVNYDfVSF--PTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNC 218
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
10-284 3.15e-23

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 98.91  E-value: 3.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDD-DKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKK-RWYLVFEFVDHTI 87
Cdd:cd14163    8 IGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGpEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVMELAEDGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVsQSGVVKLCDFGFARTLAAPG-EVYTDYVATRW 166
Cdd:cd14163   88 VFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGGrELSQTFCGSTA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 YRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQlyhiMMClgnliprHQElfnknpvfAGVRLPEiker 246
Cdd:cd14163  167 YAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPF-DDTDIPK----MLC-------QQQ--------KGVSLPG---- 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 578809600 247 eplerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14163  223 ------HLGVSRTCQDLLKRLLEPDMVLRPSIEEVSWH 254
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
2-286 3.24e-23

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 99.36  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06642    4 ELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIdLEEAEDEI--EDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd06642   82 EYLGGGSALDL-LKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdSDIdqlyHIMMCLgNLIPRhqelfNKNPVFAGvrl 240
Cdd:cd06642  161 FVGTPFWMAPE-VIKQSAYDFKADIWSLGITAIELAKGEPPN---SDL----HPMRVL-FLIPK-----NSPPTLEG--- 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 241 peiKEREPLErrypklsevviDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06642  224 ---QHSKPFK-----------EFVEACLNKDPRFRPTAKELLKHKF 255
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
2-286 3.50e-23

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 99.35  E-value: 3.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVkkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06645   11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIkLEPGEDFAV---VQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd06645   88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLVGDVK--YGKAVDVWAIGCLVTEMFMGEPlfpgdsdidqlyhimmclgnliprhqELFNKNPVFAGV 238
Cdd:cd06645  168 FIGTPYWMAPEVAAVERKggYNQLCDIWAVGITAIELAELQP--------------------------PMFDLHPMRALF 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 239 RLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06645  222 LMTKSNFQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLLQHPF 269
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
4-214 4.76e-23

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 98.92  E-value: 4.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14195    7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKfikkRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV----VKLCDFGFARTLAApG 155
Cdd:cd14195   87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFGIAHKIEA-G 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 156 EVYTDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd14195  166 NEFKNIFGTPEFVAPE-IVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNI 223
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
2-281 4.92e-23

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 99.41  E-value: 4.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMK-----CRNKDTGRI-VAIKKFLESDDDKMVKKIaMREIKLLKQL-RHENLVNLLEVCKKKK 74
Cdd:cd05053   12 DRLTLGKPLGEGAFGQVVKaeavgLDNKPNEVVtVAVKMLKDDATEKDLSDL-VSEMEMMKMIgKHKNIINLLGACTQDG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVDHTILDDlelF-----PNGLDY----------QVVQKYL----FQIINGIGFCHSHNIIHRDIKPENILVS 135
Cdd:cd05053   91 PLYVVVEYASKGNLRE---FlrarrPPGEEAspddprvpeeQLTQKDLvsfaYQVARGMEYLASKKCIHRDLAARNVLVT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 136 QSGVVKLCDFGFARTLAapgevYTDY--------VATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMFM--GEPlFPGd 205
Cdd:cd05053  168 EDNVMKIADFGLARDIH-----HIDYyrkttngrLPVKWM-APEALFDRV-YTHQSDVWSFGVLLWEIFTlgGSP-YPG- 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 206 sdidqlyhimmclgnlIPRHqELFNKnpvfagvrlpeIKEREPLERryPKL-SEVVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd05053  239 ----------------IPVE-ELFKL-----------LKEGHRMEK--PQNcTQELYMLMRDCWHEVPSQRPTFKQL 285
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
10-284 4.97e-23

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 98.33  E-value: 4.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSF----LKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-----GVVKlcDFGFARTL-------AAPGE 156
Cdd:cd14065   77 ELLKSMDeQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREAnrgrnAVVA--DFGLAREMpdektkkPDRKK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTdYVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPlfpgdSDIDQLyhimmclgnliPRHQELfnknpvfa 236
Cdd:cd14065  155 RLT-VVGSPYWMAPEMLRGES-YDEKVDVFSFGIVLCEIIGRVP-----ADPDYL-----------PRTMDF-------- 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 237 GVRLPEIKEREPlerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14065  209 GLDVRAFRTLYV-----PDCPPSFLPLAIRCCQLDPEKRPSFVELEHH 251
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
3-284 5.57e-23

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 98.37  E-value: 5.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14087    2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMI---ETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV---VKLCDFGFARTL-AAPGEVY 158
Cdd:cd14087   79 ATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRkKGPNCLM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGepLFPGDSDidqlyhimmclgNLIPRHQELFNKNPVFAGv 238
Cdd:cd14087  159 KTTCGTPEYIAPEILL-RKPYTQSVDMWAVGVIAYILLSG--TMPFDDD------------NRTRLYRQILRAKYSYSG- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 239 rlpeikerEPlerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14087  223 --------EP----WPSVSNLAKDFIDRLLTVNPGERLSATQALKH 256
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-203 5.59e-23

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 98.88  E-value: 5.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMrEIKLLKQLRHENLVNLLEVCKKKKRW------YLVFEFV 83
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCL-EIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDD-LELFPN--GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLAApGEV 157
Cdd:cd14038   81 QGGDLRKyLNQFENccGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKELDQ-GSL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 158 YTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMG-EPLFP 203
Cdd:cd14038  160 CTSFVGTLQYLAPELL-EQQKYTVTVDYWSFGTLAFECITGfRPFLP 205
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
9-210 5.83e-23

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 98.25  E-value: 5.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK-----KFLESDDDKMvkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd14082   10 VLGSGQFGIVYGGKHRKTGRDVAIKvidklRFPTKQESQL-----RNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLELFPNGLDYQVVQKYLF-QIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLaapGE--V 157
Cdd:cd14082   85 HGDMLEMILSSEKGRLPERITKFLVtQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARII---GEksF 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 158 YTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQ 210
Cdd:cd14082  162 RRSVVGTPAYLAPEVLRNK-GYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIND 213
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-287 7.62e-23

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 100.49  E-value: 7.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM--VKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD--- 84
Cdd:cd05600   19 VGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLneVNHV-LTERDILTTTNSPWLVKLLYAFQDPENVYLAMEYVPggd 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 -HTILDDLELfpngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-------------T 150
Cdd:cd05600   98 fRTLLNNSGI----LSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesmkiR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTDY------------------------VATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd05600  174 LEEVKNTAFLEltakerrniyramrkedqnyansvVGSPDYMAPEVLRGE-GYDLTVDYWSLGCILFECLVGFPPFSGST 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 207 DID---QLYHIMMCLgnliprhqelfnKNPVFAGVRLPeikereplerryPKLSEVVIDLAKKCLhIDPDKRpFCA--EL 281
Cdd:cd05600  253 PNEtwaNLYHWKKTL------------QRPVYTDPDLE------------FNLSDEAWDLITKLI-TDPQDR-LQSpeQI 306

                 ....*.
gi 578809600 282 LHHDFF 287
Cdd:cd05600  307 KNHPFF 312
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
10-206 7.93e-23

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 98.01  E-value: 7.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKM-VKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14117   14 LGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEYAPRGEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDlELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFarTLAAPGEVYTDYVATRWY 167
Cdd:cd14117   94 YK-ELQKHGrFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGW--SVHAPSLRRRTMCGTLDY 170
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809600 168 RAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd14117  171 LPPEMIEGRT-HDEKVDLWCIGVLCYELLVGMPPFESAS 208
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-284 9.59e-23

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 97.95  E-value: 9.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdddKMVKKIAMREIKLLKQLRHENLV----------NLLEVCKKK 73
Cdd:cd14047    8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRV------KLNNEKAEREVKALAKLDHPNIVryngcwdgfdYDPETSSSN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 ----KRWYLV--FEFVDHTILDDL--ELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd14047   82 ssrsKTKCLFiqMEFCEKGTLESWieKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARTLAAPGEVyTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFmgeplfpgdsdidqlyHIMmclgnliprh 225
Cdd:cd14047  162 GLVTSLKNDGKR-TKSKGTLSYMSPEQISSQ-DYGKEVDIYALGLILFELL----------------HVC---------- 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 226 QELFNKNPVFAGVR---LPEIkerepLERRYPKLSEVVidlaKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14047  214 DSAFEKSKFWTDLRngiLPDI-----FDKRYKIEKTII----KKMLSKKPEDRPNASEILRT 266
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
2-288 1.09e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 98.22  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEvckkkkrwYLVFE 81
Cdd:cd06618   15 NDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYG--------YFITD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 F-------VDHTILDDL-ELFPNGLDYQVVQKYLFQIINGIGFC-HSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLa 152
Cdd:cd06618   87 SdvficmeLMSTCLDKLlKRIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGISGRL- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 apgevyTDYVA-TRW-----YRAPELLVGDV--KYGKAVDVWAIGCLVTEMFMGEPLFPG-DSDIDQLYHIMmclgnlip 223
Cdd:cd06618  166 ------VDSKAkTRSagcaaYMAPERIDPPDnpKYDIRADVWSLGISLVELATGQFPYRNcKTEFEVLTKIL-------- 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 224 rhqelfNKNPvfagvrlPEIKEREplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06618  232 ------NEEP-------PSLPPNE-------GFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
2-286 1.19e-22

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 98.16  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLES--DDDKMVKKiamrEIKLLKQLR-HENLVNLLEVCKKKK---- 74
Cdd:cd06638   18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPihDIDEEIEA----EYNILKALSdHPNVVKFYGMYYKKDvkng 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 -RWYLVFEFVDHTILDDLE--LFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd06638   93 dQLWLVLELCNGGSVTDLVkgFLKRGerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAPGEVYTDYVATRWYRAPELLVG----DVKYGKAVDVWAIGclVTEMFMGEplfpGDSDIDQLyHIMMCLGNlIPRh 225
Cdd:cd06638  173 QLTSTRLRRNTSVGTPFWMAPEVIACeqqlDSTYDARCDVWSLG--ITAIELGD----GDPPLADL-HPMRALFK-IPR- 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 226 qelfnkNPvfagvrlpeikerePLERRYPKL-SEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06638  244 ------NP--------------PPTLHQPELwSNEFNDFIRKCLTKDYEKRPTVSDLLQHVF 285
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
10-275 1.22e-22

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 98.08  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----NKDTGRIVAIKKFLESDDDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKK--KRWYLVFEFV 83
Cdd:cd05079   12 LGEGHFGKVELCRydpeGDNTGEQVAVKSLKPESGGNHIADLK-KEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDdlELFP---NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT- 159
Cdd:cd05079   91 PSGSLK--EYLPrnkNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTv 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 --DYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMfmgepLFPGDSDIDQLYHIMMCLGnliPRHQELfnknPVFAG 237
Cdd:cd05079  169 kdDLDSPVFWYAPECLI-QSKFYIASDVWSFGVTLYEL-----LTYCDSESSPMTLFLKMIG---PTHGQM----TVTRL 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 578809600 238 VRLPEIKEREPlerRYPKLSEVVIDLAKKCLHIDPDKR 275
Cdd:cd05079  236 VRVLEEGKRLP---RPPNCPEEVYQLMRKCWEFQPSKR 270
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
2-284 1.22e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 98.94  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDkmvkkiAMREIK-LLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14176   19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD------PTEEIEiLLRYGQHPNIITLKDVYDDGKYVYVVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL-VSQSG---VVKLCDFGFARTLAAPGE 156
Cdd:cd14176   93 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQLYHIMMCLGNliprhqelfNKNPVFA 236
Cdd:cd14176  173 LLMTPCYTANFVAPEVLERQ-GYDAACDIWSLGVLLYTMLTGYTPFANGPD-DTPEEILARIGS---------GKFSLSG 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 237 GVrlpeikereplerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14176  242 GY--------------WNSVSDTAKDLVSKMLHVDPHQRLTAALVLRH 275
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
10-287 1.31e-22

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 97.16  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDdkMVKKIAMREIKLLKQLRHENLVNLLEVCKKKK-RWYLVFEFVDH 85
Cdd:cd14165    9 LGEGSYAKVKSAYSERLKCNVAIKiidKKKAPDD--FVEKFLPRELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TilDDLELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE----VYT 159
Cdd:cd14165   87 G--DLLEFIKLRgaLPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDENgrivLSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFpGDSDIDQLYHIMMclgnlipRHQELFNKNPVFAGvr 239
Cdd:cd14165  165 TFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPY-DDSNVKKMLKIQK-------EHRVRFPRSKNLTS-- 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 240 lpEIKereplerrypklsevviDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14165  235 --ECK-----------------DLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
9-202 1.44e-22

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 97.96  E-value: 1.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTgrIVAIKKFLESDDDKM--VKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF-VDH 85
Cdd:cd14158   22 KLGEGGFGVVFKGYINDK--NVAVKKLAAMVDISTedLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYmPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLELFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE-VYTD-Y 161
Cdd:cd14158  100 SLLDRLACLNDTPPLSWHMrcKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQtIMTErI 179
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809600 162 VATRWYRAPELLVGDVKygKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14158  180 VGTTAYMAPEALRGEIT--PKSDIFSFGVVLLEIITGLPPV 218
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
4-207 1.50e-22

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 98.53  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESD-------DDKMVKKiamREIKLLKQLRHENLVNLLEVCKKKKRW 76
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDiiardevESLMCEK---RIFETVNSARHPFLVNLFACFQTPEHV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFvdhTILDDL------ELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd05589   78 CFVMEY---AAGGDLmmhiheDVFSE----PRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKE 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 151 LAAPGEVYTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSD 207
Cdd:cd05589  151 GMGFGDRTSTFCGTPEFLAPEVLT-DTSYTRAVDWWGLGVLIYEMLVGESPFPGDDE 206
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
4-206 2.17e-22

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 96.58  E-value: 2.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLesdDDKMVKKIAM-REIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14113    9 YSEVAELGRGRFSVVKKCDQRGTKRAVATK-FV---NKKLMKRDQVtHELGVLQSLQHPQLVGLLDTFETPTSYILVLEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLAAPGEVYt 159
Cdd:cd14113   85 ADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFGDAVQLNTTYYIH- 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 160 DYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd14113  164 QLLGSPEFAAPEIILGN-PVSLTSDLWSIGVLTYVLLSGVSPFLDES 209
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
10-276 2.34e-22

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 98.03  E-value: 2.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVKK------IAMREIkLLKQLRHEN--LVNLLEVCKKKKRWYLVFE 81
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVL---SKKVIVAKkevahtIGERNI-LVRTALDESpfIVGLKFSFQTPTDLYLVTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTilddlELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd05586   77 YMSGG-----ELFwhlqkEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMG-EPLFPgdSDIDQLYHiMMCLGNL-IPRH--------- 225
Cdd:cd05586  152 TTNTFCGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGwSPFYA--EDTQQMYR-NIAFGKVrFPKDvlsdegrsf 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 226 -QELFNKNPVFagvRLPEIKEREPLeRRYPKLSEVVIDLAKKCLhIDPDKRP 276
Cdd:cd05586  229 vKGLLNRNPKH---RLGAHDDAVEL-KEHPFFADIDWDLLSKKK-ITPPFKP 275
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-289 2.42e-22

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 97.51  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLL-------EVCkkkk 74
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMA-RKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYgafysdgEIS---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 rwyLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHS-HNIIHRDIKPENILVSQSGVVKLCDFGFARTLAa 153
Cdd:cd06615   76 ---ICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 pGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGE-PLFPGDSdiDQLYHIMMCLGNLIPRHQELFNKN 232
Cdd:cd06615  152 -DSMANSFVGTRSYMSPERLQGT-HYTVQSDIWSLGLSLVEMAIGRyPIPPPDA--KELEAMFGRPVSEGEAKESHRPVS 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 233 PVFAGVRLP--------EIKEREPlerryPKL-----SEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06615  228 GHPPDSPRPmaifelldYIVNEPP-----PKLpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKR 292
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-215 2.48e-22

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 98.22  E-value: 2.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK---KFlesdddKMVKKIAM------REIkllkqLRHEN---LVNLLEV 69
Cdd:cd05596   26 EDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKllsKF------EMIKRSDSaffweeRDI-----MAHANsewIVQLHYA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  70 CKKKKRWYLVFEFVDH----TILDDLElFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd05596   95 FQDDKYLYMVMDYMPGgdlvNLMSNYD-VPE----KWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADF 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 146 GFARTLAAPGEVYTDY-VATRWYRAPELLV---GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM 215
Cdd:cd05596  170 GTCMKMDKDGLVRSDTaVGTPDYISPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIM 243
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
11-295 2.70e-22

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 96.88  E-value: 2.70e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKkflesdddkMVKKIAMR--------EIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14169   12 GEGAFSEVVLAQERGSQRLVALK---------CIPKKALRgkeamvenEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAapGEVYT 159
Cdd:cd14169   83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIEA--QGMLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQLYhimmclgNLIPRHQELFNkNPVfagvr 239
Cdd:cd14169  161 TACGTPGYVAPELL-EQKPYGKAVDVWAIGVISYILLCGYPPFYDEND-SELF-------NQILKAEYEFD-SPY----- 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 240 lpeikereplerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMDGFAER 295
Cdd:cd14169  226 -------------WDDISESAKDFIRHLLERDPEKRFTCEQALQHPWISGDTALDR 268
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1-284 3.01e-22

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 96.53  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLV-----GEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHE-NLVNLLEVCKKKK 74
Cdd:cd14198    2 MDNFNNFYILtskelGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNpRVVNLHEVYETTS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFV------DHTILDDLELFPNGldyQVVqKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS---GVVKLCDF 145
Cdd:cd14198   82 EIILILEYAaggeifNLCVPDLAEMVSEN---DII-RLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARTLAAPGEVyTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprh 225
Cdd:cd14198  158 GMSRKIGHACEL-REIMGTPEYLAPEILNYD-PITTATDMWNIGVIAYMLLTHESPFVGEDN------------------ 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 226 QELF-NKNPVfagvrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14198  218 QETFlNISQV----------NVDYSEETFSSVSQLATDFIQKLLVKNPEKRPTAEICLSH 267
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
11-202 3.66e-22

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 96.66  E-value: 3.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKfLESdddKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFefvdh 85
Cdd:cd05605    9 GKGGFGEVCACQVRATGKMYACKK-LEK---KRIKKrkgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVL----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILD--DLE-----LFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaAPGEVY 158
Cdd:cd05605   80 TIMNggDLKfhiynMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEI-PEGETI 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578809600 159 TDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05605  159 RGRVGTVGYMAPE-VVKNERYTFSPDWWGLGCLIYEMIEGQAPF 201
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
10-284 4.02e-22

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 96.43  E-value: 4.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDdkmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTild 89
Cdd:cd14085   11 LGRGATSVVYRCRQKGTQKPYAVKKLKKTVD----KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGG--- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 dlELFPngldyQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLaaPGE 156
Cdd:cd14085   84 --ELFD-----RIVEKGYYserdaadavkQILEAVAYLHENGIVHRDLKPENLLYATPApdaPLKIADFGLSKIV--DQQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYV-ATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG-EPLFPGDSDIDQLYHIMMClgnliprhqelfnknpv 234
Cdd:cd14085  155 VTMKTVcGTPGYCAPEILRGC-AYGPEVDMWSVGVITYILLCGfEPFYDERGDQYMFKRILNC----------------- 216
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 235 fagvrlpeikEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14085  217 ----------DYDFVSPWWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQH 256
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-205 5.14e-22

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 95.77  E-value: 5.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLkQLRHENL--VNLLEVCKKKKRWYLVFEFV---- 83
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVL-ELAQANPwvINLHEVYETASEMILVLEYAagge 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 --DHTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS---GVVKLCDFGFARTLAAPGEVy 158
Cdd:cd14197   96 ifNQCVADREEAFKE----KDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSRILKNSEEL- 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 159 TDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGD 205
Cdd:cd14197  171 REIMGTPEYVAPEILSYE-PISTATDMWSIGVLAYVMLTGISPFLGD 216
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-286 5.44e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 95.57  E-value: 5.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKdtgrivaikKFLESDDDKMVKKI------------AMREIKLLKQLRHENLVNLLEVC 70
Cdd:cd08222    1 RYRVVRKLGSGNFGTVYLVSDL---------KATADEELKVLKEIsvgelqpdetvdANREAKLLSKLDHPAIVKFHDSF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  71 KKKKRWYLVFEFVDHTILDDL--ELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQsGVVKLCDFG 146
Cdd:cd08222   72 VEKESFCIVTEYCEGGDLDDKisEYKKSGttIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTLAAPGEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmCLGNliprhq 226
Cdd:cd08222  151 ISRILMGTSDLATTFTGTPYYMSPEVLKH-EGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKI--VEGE------ 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 227 elfnknpvfagvrLPEIKEREPLERRypklsevviDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd08222  222 -------------TPSLPDKYSKELN---------AIYSRMLNKDPALRPSAAEILKIPF 259
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
2-286 5.51e-22

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 95.89  E-value: 5.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd06640    4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIdLEEAEDEI--EDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDH-TILDDLELFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd06640   82 EYLGGgSALDLLRAGP--FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEplfPGDSDIdqlyHIMMCLgNLIPRhqelfNKNPVFAGVR 239
Cdd:cd06640  160 TFVGTPFWMAPE-VIQQSAYDSKADIWSLGITAIELAKGE---PPNSDM----HPMRVL-FLIPK-----NNPPTLVGDF 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 240 LPEIKEreplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd06640  226 SKPFKE-----------------FIDACLNKDPSFRPTAKELLKHKF 255
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
9-215 6.16e-22

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 96.79  E-value: 6.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKmvkKIAMREIKLLK-QLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05591    2 VLGKGSFGKVMLAERKGTDEVYAIKvlkkDVILQDDDV---DCTMTEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 dhtilddlelfpNGLD--YQVvQK-----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd05591   79 ------------NGGDlmFQI-QRarkfdeprarfYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKE 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 151 LAAPGEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM 215
Cdd:cd05591  146 GILNGKTTTTFCGTPDYIAPEIL-QELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESIL 209
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
10-276 6.18e-22

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 95.19  E-value: 6.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRiVAIKKFleSDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd05148   14 LGSGYFGEVWEGLWKNRVR-VAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVVQKYLF--QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgeVYTDY---VAT 164
Cdd:cd05148   91 AFLRSPEGQVLPVASLIDMacQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKED--VYLSSdkkIPY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWyRAPELLvGDVKYGKAVDVWAIGCLVTEMFM-GEPLFPGDSDidqlyhimmclgnliprhQELFNKnpVFAGVRLPei 243
Cdd:cd05148  169 KW-TAPEAA-SHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNN------------------HEVYDQ--ITAGYRMP-- 224
                        250       260       270
                 ....*....|....*....|....*....|...
gi 578809600 244 kereplerRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd05148  225 --------CPAKCPQEIYKIMLECWAAEPEDRP 249
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
4-283 6.31e-22

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 95.37  E-value: 6.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKmvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF- 82
Cdd:cd14110    5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDK---QLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELc 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELfPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL----AAPGEVY 158
Cdd:cd14110   82 SGPELLYNLAE-RNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFnqgkVLMTDKK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATrwyRAPELLVGDvKYGKAVDVWAIGclVTEMFMGEPLFPGDSDidqlyhimmclgnlIPRHQElfnknpvfAGV 238
Cdd:cd14110  161 GDYVET---MAPELLEGQ-GAGPQTDIWAIG--VTAFIMLSADYPVSSD--------------LNWERD--------RNI 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 239 RLPEIKerepLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd14110  213 RKGKVQ----LSRCYAGLSGGAVNFLKSTLCAKPWGRPTASECLQ 253
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
9-208 6.37e-22

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 95.30  E-value: 6.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVK----KIAMREIKLLKQL----RHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14101    7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKlpgvNPVPNEVALLQSVgggpGHRGVIRLLDWFEIPEGFLLVL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTI-LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS-QSGVVKLCDFGFARTLAapGEVY 158
Cdd:cd14101   87 ERPQHCQdLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFGSGATLK--DSMY 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDI 208
Cdd:cd14101  165 TDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERDTDI 214
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
9-216 6.99e-22

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 96.51  E-value: 6.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-----LESDDdkmvKKIAMREIKLLKQLRHENLVNLLEVC-KKKKRWYLVFEF 82
Cdd:cd05590    2 VLGKGSFGKVMLARLKESGRLYAVKVLkkdviLQDDD----VECTMTEKRILSLARNHPFLTQLYCCfQTPDRLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILddleLF----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd05590   78 VNGGDL----MFhiqkSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTT 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 159 TDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQLYHIMM 216
Cdd:cd05590  154 STFCGTPDYIAPEIL-QEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENE-DDLFEAIL 209
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
10-214 7.00e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 95.07  E-value: 7.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV------ 83
Cdd:cd14191   10 LGSGKFGQVFRLVEKKTKKVWA-GKFFKAYSAKEKENI-RQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVsggelf 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLELfpngLDYQVVqKYLFQIINGIGFCHSHNIIHRDIKPENIL-VSQSGV-VKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd14191   88 ERIIDEDFEL----TERECI-KYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGTkIKLIDFGLARRLENAGSLKVLF 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 162 vATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd14191  163 -GTPEFVAPEVINYE-PIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV 213
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
4-288 7.85e-22

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 95.94  E-value: 7.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKiamrEIKLLKQL-RHENLVNLLEVCKKKK------R 75
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMdVTGDEEEEIKQ----EINMLKKYsHHRNIATYYGAFIKKNppgmddQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHTILDDL--ELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd06637   84 LWLVMEFCGAGSVTDLikNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDYVATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYhimmclgnLIPRhqelf 229
Cdd:cd06637  164 TVGRRNTFIGTPYWMAPEVIAcdenPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALF--------LIPR----- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 230 nkNPVfagvrlPEIKEReplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06637  231 --NPA------PRLKSK--------KWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR 273
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
10-284 8.73e-22

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 95.47  E-value: 8.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESdddkmvKKIAMREIK-LLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14178   11 IGIGSYSVCKRCVHKATSTEYAVKIIDKS------KRDPSEEIEiLLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL-VSQSG---VVKLCDFGFARTLAAPGEVYTDYVAT 164
Cdd:cd14178   85 LDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGnpeSIRICDFGFAKQLRAENGLLMTPCYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDiDQLYHIMMCLGNliprhqelfNKNPVFAGvrlpeik 244
Cdd:cd14178  165 ANFVAPEVLKRQ-GYDAACDIWSLGILLYTMLAGFTPFANGPD-DTPEEILARIGS---------GKYALSGG------- 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578809600 245 ereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14178  227 -------NWDSISDAAKDIVSKMLHVDPHQRLTAPQVLRH 259
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
2-287 8.76e-22

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 96.23  E-value: 8.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRI-VAIK------KFLESdddkmvkkiAMREIKLLKQLRHENLVNLLeVCKKKK 74
Cdd:cd14214   13 ERYEIVGDLGEGTFGKVVECLDHARGKSqVALKiirnvgKYREA---------ARLEINVLKKIKEKDKENKF-LCVLMS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWylvFEFVDHTILDDLELFPNGLDYQVVQKYL-----------FQIINGIGFCHSHNIIHRDIKPENILVSQS------ 137
Cdd:cd14214   83 DW---FNFHGHMCIAFELLGKNTFEFLKENNFQpyplphirhmaYQLCHALKFLHENQLTHTDLKPENILFVNSefdtly 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 138 -------------GVVKLCDFGFArtlAAPGEVYTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPG 204
Cdd:cd14214  160 nesksceeksvknTSIRVADFGSA---TFDHEHHTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQT 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 205 DSDIDQLYHIMMCLGNlIPRH-------QELFNKNPVFAGVRLPE---IKER-EPLeRRYpKLSEV-----VIDLAKKCL 268
Cdd:cd14214  236 HENREHLVMMEKILGP-IPSHmihrtrkQKYFYKGSLVWDENSSDgryVSENcKPL-MSY-MLGDSlehtqLFDLLRRML 312
                        330
                 ....*....|....*....
gi 578809600 269 HIDPDKRPFCAELLHHDFF 287
Cdd:cd14214  313 EFDPALRITLKEALLHPFF 331
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
7-216 1.07e-21

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 95.84  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESD----DDKMvkKIAMREIKLLKQLRHENLVNLLEVC-KKKKRWYLVFE 81
Cdd:cd05616    5 LMVLGKGSFGKVMLAERKGTDELYAVK-ILKKDvviqDDDV--ECTMVEKRVLALSGKPPFLTQLHSCfQTMDRLYFVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVdhtilddlelfpNGLD--YQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd05616   82 YV------------NGGDlmYHIQQVgrfkephavfYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 150 TLAAPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDsDIDQLYHIMM 216
Cdd:cd05616  150 ENIWDGVTTKTFCGTPDYIAPEIIAYQ-PYGKSVDWWAFGVLLYEMLAGQAPFEGE-DEDELFQSIM 214
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
10-282 1.24e-21

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 94.51  E-value: 1.24e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLES-DDDKMVkkiamREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDvDQHKIV-----REISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLeLFPNGLDYQVVQKYLF--QIINGIGFCHSHNIIHRDIKPENILVSQSGVVK---LCDFGFARTL----AAPGEVYT 159
Cdd:cd14156   76 EEL-LAREELPLSWREKVELacDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempANDPERKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFmgePLFPGDSDIdqlyhimmclgnlIPRHQELfnknpvfaGVR 239
Cdd:cd14156  155 SLVGSAFWMAPEMLRGE-PYDRKVDVFSFGIVLCEIL---ARIPADPEV-------------LPRTGDF--------GLD 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578809600 240 LPEIKEreplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd14156  210 VQAFKE------MVPGCPEPFLDLAASCCRMDAFKRPSFAELL 246
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-247 1.31e-21

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 94.28  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDD--DKMVKkiamREIKLLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14665    1 RYELVKDIGSGNFGVARLMRDKQTKELVAVK-YIERGEkiDENVQ----REIINHRSLRHPNIVRFKEVILTPTHLAIVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILddLELFPNGLDYQVVQKYLF--QIINGIGFCHSHNIIHRDIKPENILVSQSGV--VKLCDFGFARTLAAPGE 156
Cdd:cd14665   76 EYAAGGEL--FERICNAGRFSEDEARFFfqQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDyVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMG-----EPLFPGD------------SDIDQLYHIMMCLG 219
Cdd:cd14665  154 PKST-VGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGaypfeDPEEPRNfrktiqrilsvqYSIPDYVHISPECR 232
                        250       260
                 ....*....|....*....|....*...
gi 578809600 220 NLIPRhqeLFNKNPVfAGVRLPEIKERE 247
Cdd:cd14665  233 HLISR---IFVADPA-TRITIPEIRNHE 256
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
10-284 1.55e-21

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 94.86  E-value: 1.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKC-----RNKDTGRIVAIKkFLESDDDKMVKKIAMREIKLLKQL-RHENLVNLLEVC-KKKKRWYLVFEF 82
Cdd:cd05054   15 LGRGAFGKVIQAsafgiDKSATCRTVAVK-MLKEGATASEHKALMTELKILIHIgHHLNVVNLLGACtKPGGPLMVIVEF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTIL--------------------------DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQ 136
Cdd:cd05054   94 CKFGNLsnylrskreefvpyrdkgardveeeeDDDELYKEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 137 SGVVKLCDFGFARtlaapgEVYT--DYVAT-------RWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGdS 206
Cdd:cd05054  174 NNVVKICDFGLAR------DIYKdpDYVRKgdarlplKWM-APESIFDKV-YTTQSDVWSFGVLLWEIFsLGASPYPG-V 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 207 DIDqlyhimmclgnliprhQELFNKnpVFAGVRLpeikeREPlERRYPKLSEVVIDlakkCLHIDPDKRPFCAELLHH 284
Cdd:cd05054  245 QMD----------------EEFCRR--LKEGTRM-----RAP-EYTTPEIYQIMLD----CWHGEPKERPTFSELVEK 294
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
11-251 1.62e-21

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 95.53  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKF-----LESDDDK--MVKKiamREIKLLKQlrHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05592    4 GKGSFGKVMLAELKGTNQYFAIKALkkdvvLEDDDVEctMIER---RVLALASQ--HPFLTHLFCTFQTESHLFFVMEYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 dhtilddlelfpNGLD--YQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTl 151
Cdd:cd05592   79 ------------NGGDlmFHIQQSgrfdedrarfYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKE- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 aapgEVYTDYVATRW-----YRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDsDIDQLYHIMMclgnliprhq 226
Cdd:cd05592  146 ----NIYGENKASTFcgtpdYIAPEILKGQ-KYNQSVDWWSFGVLLYEMLIGQSPFHGE-DEDELFWSIC---------- 209
                        250       260       270
                 ....*....|....*....|....*....|..
gi 578809600 227 elfNKNPVF-------AGVRLPEIKEREPLER 251
Cdd:cd05592  210 ---NDTPHYprwltkeAASCLSLLLERNPEKR 238
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
2-287 1.68e-21

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 95.47  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRN-KDTGRIVAIK--KFLESdddkmVKKIAMREIKLLKQLRHENLVNLlEVCKKKKRWY- 77
Cdd:cd14215   12 ERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKiiKNVEK-----YKEAARLEINVLEKINEKDPENK-NLCVQMFDWFd 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 ------LVFEFVDHTILDDLELfPNGLDYQV--VQKYLFQIINGIGFCHSHNIIHRDIKPENIL---------------- 133
Cdd:cd14215   86 yhghmcISFELLGLSTFDFLKE-NNYLPYPIhqVRHMAFQVCQAVKFLHDNKLTHTDLKPENILfvnsdyeltynlekkr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 134 ---VSQSGVVKLCDFGFArtlAAPGEVYTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQ 210
Cdd:cd14215  165 derSVKSTAIRVVDFGSA---TFDHEHHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 211 LYHIMMCLGNLIPRHQELFNKNPVFAGVRLP---------EIKER-EPLeRRYpKLSEV-----VIDLAKKCLHIDPDKR 275
Cdd:cd14215  241 LAMMERILGPIPSRMIRKTRKQKYFYHGRLDwdentsagrYVRENcKPL-RRY-LTSEAeehhqLFDLIESMLEYEPSKR 318
                        330
                 ....*....|..
gi 578809600 276 PFCAELLHHDFF 287
Cdd:cd14215  319 LTLAAALKHPFF 330
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2-205 1.92e-21

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 93.73  E-value: 1.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVaIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14111    3 KPYTFLDEKARGRFGVIRRCRENATGKNF-PAKIVPYQAEE--KQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVD-----HTILDDLELFPNGldyqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd14111   80 FCSgkellHSLIDRFRYSEDD-----VVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSL 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 157 VYTD-YVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGE-PLFPGD 205
Cdd:cd14111  155 RQLGrRTGTLEYMAPEMVKGEP-VGPPADIWSIGVLTYIMLSGRsPFEDQD 204
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
2-287 2.27e-21

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 95.30  E-value: 2.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKD-TGRIVAIKKFLESDddkMVKKIAMREIKLLKQLRHENLVNLLEvCKKKKRWY--- 77
Cdd:cd14213   12 ARYEIVDTLGEGAFGKVVECIDHKmGGMHVAVKIVKNVD---RYREAARSEIQVLEHLNTTDPNSTFR-CVQMLEWFdhh 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 ----LVFEFVDHTILDDLE---LFPNGLDYqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV----------- 139
Cdd:cd14213   88 ghvcIVFELLGLSTYDFIKensFLPFPIDH--IRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYvvkynpkmkrd 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 140 --------VKLCDFGFArtlAAPGEVYTDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQL 211
Cdd:cd14213  166 ertlknpdIKVVDFGSA---TYDDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 212 YHIMMCLGNlIPRHQ-ELFNKNPVFAGVRLPEIKEREP---LERRYPKLSEVVI----------DLAKKCLHIDPDKRPF 277
Cdd:cd14213  242 AMMERILGP-LPKHMiQKTRKRKYFHHDQLDWDEHSSAgryVRRRCKPLKEFMLsqdvdheqlfDLIQKMLEYDPAKRIT 320
                        330
                 ....*....|
gi 578809600 278 CAELLHHDFF 287
Cdd:cd14213  321 LDEALKHPFF 330
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
11-287 2.47e-21

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 93.88  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMkCRNKDTGRIVAIKKFLESDDDkmvkkIAMREIKLLKQL-RHENLVNLLevCKKKKR--WYLVFEFVDHTi 87
Cdd:cd13982   10 GYGSEGTIV-FRGTFDGRPVAVKRLLPEFFD-----FADREVQLLRESdEHPNVIRYF--CTEKDRqfLYIALELCAAS- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDL----ELFP----NGLDyqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV-----VKLCDFGFARTLAAP 154
Cdd:cd13982   81 LQDLvespRESKlflrPGLE---PVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLDVG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVY--TDYVA-TRWYRAPELLVGDVKYG--KAVDVWAIGCL----VTemfMGEPLFpGDSdidqlyhiMMCLGNLiprh 225
Cdd:cd13982  158 RSSFsrRSGVAgTSGWIAPEMLSGSTKRRqtRAVDIFSLGCVfyyvLS---GGSHPF-GDK--------LEREANI---- 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 226 qelfnknpvfagvrlpeIKEREPLERRYPKLSEVVI--DLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd13982  222 -----------------LKGKYSLDKLLSLGEHGPEaqDLIERMIDFDPEKRPSAEEVLNHPFF 268
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
1-288 2.60e-21

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 94.03  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGlvgEGSYGMVMKCRNKDTGRIVAIKKF---LESDDDK---MVKKIAMREIKLlkqlrhENLVNLLEVCKKKK 74
Cdd:cd06617    3 LEVIEELG---RGAYGVVDKMRHVPTGTIMAVKRIratVNSQEQKrllMDLDISMRSVDC------PYTVTFYGALFREG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVDhTILDDLelFPNGLDYQ------VVQKYLFQIINGIGFCHSH-NIIHRDIKPENILVSQSGVVKLCDFGF 147
Cdd:cd06617   74 DVWICMEVMD-TSLDKF--YKKVYDKGltipedILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 148 ARTLaapgevyTDYVA------TRWYRAPELLVGDVK---YGKAVDVWAIGCLVTEMFMGEplFPGDS---DIDQLYHIM 215
Cdd:cd06617  151 SGYL-------VDSVAktidagCKPYMAPERINPELNqkgYDVKSDVWSLGITMIELATGR--FPYDSwktPFQQLKQVV 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 216 mclgnliprhqelfnKNPvfaGVRLPEikereplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06617  222 ---------------EEP---SPQLPA-----------EKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
9-276 2.71e-21

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 93.83  E-value: 2.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKF-------------------LESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV 69
Cdd:cd14000    1 LLGDGGFGSVYRASYK--GEPVAVKIFnkhtssnfanvpadtmlrhLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  70 CKKKKrwYLVFEF-----VDHTILDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV-----SQSGV 139
Cdd:cd14000   79 GIHPL--MLVLELaplgsLDHLLQQDSRSFAS-LGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAII 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 140 VKLCDFGFARTLAAPGEVYTDyvATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGdsdidqlyhimmclg 219
Cdd:cd14000  156 IKIADYGISRQCCRMGAKGSE--GTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVG--------------- 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 220 nliprHQELFNKNPVFAGVRlPEIKEREplERRYPKlsevVIDLAKKCLHIDPDKRP 276
Cdd:cd14000  219 -----HLKFPNEFDIHGGLR-PPLKQYE--CAPWPE----VEVLMKKCWKENPQQRP 263
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
9-287 2.85e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 94.69  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDDKMVKKIAmrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05595    2 LLGKGTFGKVILVREKATGRYYAMKilrKEVIIAKDEVAHTVT--ESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TilddlELFPNGLDYQVVQK-----YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd05595   80 G-----ELFFHLSRERVFTEdrarfYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGE-PLFPGDsdidqlyhimmclgnliprHQELFNKnpvfagVR 239
Cdd:cd05595  155 FCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQD-------------------HERLFEL------IL 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 240 LPEIkereplerRYPK-LSEVVIDLAKKCLHIDPDKR----PFCA-ELLHHDFF 287
Cdd:cd05595  209 MEEI--------RFPRtLSPEAKSLLAGLLKKDPKQRlgggPSDAkEVMEHRFF 254
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
16-288 4.16e-21

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 93.90  E-value: 4.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  16 GMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDL--E 92
Cdd:cd08216   14 GVVHLAKHKPTNTLVAVKKInLESDSKEDLKFL-QQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLlkT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  93 LFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT---DYV--ATR-- 165
Cdd:cd08216   93 HFPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKRQRvvhDFPksSEKnl 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 166 -WYrAPELLVGDVK-YGKAVDVWAIGCLVTEMFMG-EPLFpgDSDIDQLY--HIMMCLGNLIPRH----QELFNKNPVFA 236
Cdd:cd08216  173 pWL-SPEVLQQNLLgYNEKSDIYSVGITACELANGvVPFS--DMPATQMLleKVRGTTPQLLDCStyplEEDSMSQSEDS 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 237 GVRLPEIKERE--PLERRYpklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd08216  250 STEHPNNRDTRdiPYQRTF---SEAFHQFVELCLQRDPELRPSASQLLAHSFFK 300
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
5-289 4.25e-21

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 93.58  E-value: 4.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMKCRNKDTGRIVAIKKfLESDDDKmvkkiamreiKLLKQLRHEnlvnlLEVCKKKK------RWY- 77
Cdd:cd06616    9 KDLGEIGRGAFGTVNKMLHKPSGTIMAVKR-IRSTVDE----------KEQKRLLMD-----LDVVMRSSdcpyivKFYg 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILddLELFPNGLD------YQVVQKYL-FQIINGIGFC---------HSHNIIHRDIKPENILVSQSGVVK 141
Cdd:cd06616   73 ALFREGDCWIC--MELMDISLDkfykyvYEVLDSVIpEEILGKIAVAtvkalnylkEELKIIHRDVKPSNILLDRNGNIK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 142 LCDFG--------FARTLAApgevytdyvATRWYRAPELL---VGDVKYGKAVDVWAIGCLVTEMFMGEPLFPG-DSDID 209
Cdd:cd06616  151 LCDFGisgqlvdsIAKTRDA---------GCRPYMAPERIdpsASRDGYDVRSDVWSLGITLYEVATGKFPYPKwNSVFD 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 210 QLyhimmclgnliprhQELFNKNPvfagvrlPEIKEREPLERrypklSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQM 289
Cdd:cd06616  222 QL--------------TQVVKGDP-------PILSNSEEREF-----SPSFVNFVNLCLIKDESKRPKYKELLKHPFIKM 275
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-290 4.35e-21

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 92.85  E-value: 4.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR-NKDTGriVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd05068   16 LGSGQFGEVWEGLwNNTTP--VAVKTL---KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLeLFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgEVYTDYVATRW 166
Cdd:cd05068   91 LEY-LQGKGRSLQLPQliDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVE-DEYEAREGAKF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 ---YRAPELLVGDvKYGKAVDVWAIGCLVTEMFM-GEPLFPGDSD---IDQLYHimmclgnliprhqelfnknpvfaGVR 239
Cdd:cd05068  169 pikWTAPEAANYN-RFSIKSDVWSFGILLTEIVTyGRIPYPGMTNaevLQQVER-----------------------GYR 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 240 LPeikerEPlerryPKLSEVVIDLAKKCLHIDPDKRP-FcaELLH---HDFFQMD 290
Cdd:cd05068  225 MP-----CP-----PNCPPQLYDIMLECWKADPMERPtF--ETLQwklEDFFVND 267
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
3-202 5.07e-21

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 94.28  E-value: 5.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLV---GEGSYGMVMKCRNKDTG-RIVAIKKFLESD--DDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRW 76
Cdd:PTZ00426  28 KYEDFNFIrtlGTGSFGRVILATYKNEDfPPVAIKRFEKSKiiKQKQVDHV-FSERKILNYINHPFCVNLYGSFKDESYL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:PTZ00426 107 YLVLEFVIggefFTFLRRNKRFPN----DVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVD 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 ApgEVYTdYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:PTZ00426 183 T--RTYT-LCGTPEYIAPEILL-NVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
10-288 5.63e-21

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 92.70  E-value: 5.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEE--TQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA-----APGEVYTD---- 160
Cdd:cd14222   79 DFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeekkkPPPDKPTTkkrt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 -----------YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMfmgeplfpgdsdIDQLYHIMMCLgnliPRHQElF 229
Cdd:cd14222  159 lrkndrkkrytVVGNPYWMAPEMLNGK-SYDEKVDIFSFGIVLCEI------------IGQVYADPDCL----PRTLD-F 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 230 NKNpvfagVRLpeikerePLERRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELlhHDFFQ 288
Cdd:cd14222  221 GLN-----VRL-------FWEKFVPKdCPPAFFPLAAICCRLEPDSRPAFSKL--EDSFE 266
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
10-276 6.84e-21

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 93.32  E-value: 6.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRI-VAIK---KFLESDDDKMVKKIAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05055   43 LGAGAFGKVVEATAYGLSKSdAVMKvavKMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYCC 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDL-----ELFpngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgevyT 159
Cdd:cd05055  123 YGDLLNFlrrkrESF---LTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMND----S 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVA-------TRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGdsdidqlyhimmclgnlIPRHQELFnk 231
Cdd:cd05055  196 NYVVkgnarlpVKWM-APESIFNCV-YTFESDVWSYGILLWEIFsLGSNPYPG-----------------MPVDSKFY-- 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 232 NPVFAGVRL--PEIKEREplerrypklsevVIDLAKKCLHIDPDKRP 276
Cdd:cd05055  255 KLIKEGYRMaqPEHAPAE------------IYDIMKTCWDADPLKRP 289
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
2-288 7.49e-21

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 92.75  E-value: 7.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLE--SDDDKMVKKiamrEIKLLKQL-RHENLVNLLEVCKKKKRW-- 76
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVK-ILDpiSDVDEEIEA----EYNILRSLpNHPNVVKFYGMFYKADQYvg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 ---YLVFEFVDHTILDDL--ELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd06639   97 gqlWLVLELCNGGSVTELvkGLLKCGqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAPGEVYTDYVATRWYRAPELLVG----DVKYGKAVDVWAIGCLVTEMFMGEPlfpgdsdidqlyhimmclgnliprh 225
Cdd:cd06639  177 QLTSARLRRNTSVGTPFWMAPEVIACeqqyDYSYDARCDVWSLGITAIELADGDP------------------------- 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 226 qELFNKNPVFAGVRLPeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd06639  232 -PLFDMHPVKALFKIP--RNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
9-288 9.30e-21

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 92.64  E-value: 9.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05608    8 VLGKGGFGEVSACQMRATGKLYACKKL----NKKRLKKrkgyeGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 D-----HTILDDLELFPnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd05608   84 NggdlrYHIYNVDEENP-GFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGDvKYGKAVDVWAIGclVTemfmgeplfpgdsdidqLYHIMMCLGNLIPRHQELFNKnpvfagv 238
Cdd:cd05608  163 KGYAGTPGFMAPELLLGE-EYDYSVDYFTLG--VT-----------------LYEMIAARGPFRARGEKVENK------- 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 239 rlpEIKER---EPLErrYP-KLSEVVIDLAKKCLHIDPDKR-----PFCAELLHHDFFQ 288
Cdd:cd05608  216 ---ELKQRilnDSVT--YSeKFSPASKSICEALLAKDPEKRlgfrdGNCDGLRTHPFFR 269
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
10-215 1.22e-20

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 91.85  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKiamREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDhtild 89
Cdd:cd14104    8 LGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVK---KEISILNIARHRNILRLHESFESHEELVMIFEFIS----- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQV------VQKYLFQIINGIGFCHSHNIIHRDIKPENIL--VSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd14104   80 GVDIFERITTARFelnereIVSYVRQVCEALEFLHSKNIGHFDIRPENIIycTRRGSYIKIIEFGQSRQLKPGDKFRLQY 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 162 VATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM 215
Cdd:cd14104  160 TSAEFY-APEVHQHES-VSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIR 211
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
4-288 1.27e-20

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 92.37  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYG---MVMKCRNKDTGRIVAIKKFLESDDDKMVKKI--AMREIKLLKQLRHEN-LVNLLEVCKKKKRWY 77
Cdd:cd05613    2 FELLKVLGTGAYGkvfLVRKVSGHDAGKLYAMKVLKKATIVQKAKTAehTRTERQVLEHIRQSPfLVTLHYAFQTDTKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART-LA 152
Cdd:cd05613   82 LILDYINggelFTHLSQRERFTE----NEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEfLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDYVATRWYRAPELLV-GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQlyhimmclgnliprHQELFNK 231
Cdd:cd05613  158 DENERAYSFCGTIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNS--------------QAEISRR 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 232 npvfagvrlpeIKEREPlerRYPK-LSEVVIDLAKKCLHIDPDKRPFCA-----ELLHHDFFQ 288
Cdd:cd05613  224 -----------ILKSEP---PYPQeMSALAKDIIQRLLMKDPKKRLGCGpngadEIKKHPFFQ 272
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
10-199 1.28e-20

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 91.02  E-value: 1.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMkcRNKDTGRIVAIKKflesdddkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14059    1 LGSGAQGAVF--LGKFRGEEVAVKK---------VRDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapGEVYT--DYVATRWY 167
Cdd:cd14059   70 EVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL---SEKSTkmSFAGTVAW 146
                        170       180       190
                 ....*....|....*....|....*....|..
gi 578809600 168 RAPELLVGDVKYGKaVDVWAIGCLVTEMFMGE 199
Cdd:cd14059  147 MAPEVIRNEPCSEK-VDIWSFGVVLWELLTGE 177
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
9-292 1.30e-20

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 91.98  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFefv 83
Cdd:cd05631    7 VLGKGGFGEVCACQVRATGKMYACKKL----EKKRIKKrkgeaMALNEKRILEKVNSRFVVSLAYAYETKDALCLVL--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 dhTILD--DLE-----LFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApGE 156
Cdd:cd05631   80 --TIMNggDLKfhiynMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPE-GE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlyhimmclgnliPRHQELFNKNPVfa 236
Cdd:cd05631  157 TVRGRVGTVGYMAPEVINNE-KYTFSPDWWGLGCLIYEMIQGQSPF--------------------RKRKERVKREEV-- 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 237 gvrlpEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFC-----AELLHHDFFQMDGF 292
Cdd:cd05631  214 -----DRRVKEDQEEYSEKFSEDAKSICRMLLTKNPKERLGCrgngaAGVKQHPIFKNINF 269
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
3-196 1.62e-20

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 91.88  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYenLGLVGEGSYGMVMKCR----NKDTGRIVAIKKfLESDDDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKR--W 76
Cdd:cd05081    7 KY--ISQLGKGNFGSVELCRydplGDNTGALVAVKQ-LQHSGPDQQRDFQ-REIQILKALHSDFIVKYRGVSYGPGRrsL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFV-DHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaaPG 155
Cdd:cd05081   83 RLVMEYLpSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLL--PL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 156 EvyTDYVATR--------WYrAPELLVGDVkYGKAVDVWAIGCLVTEMF 196
Cdd:cd05081  161 D--KDYYVVRepgqspifWY-APESLSDNI-FSRQSDVWSFGVVLYELF 205
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
9-202 1.80e-20

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 91.50  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05607    9 VLGKGGFGEVCAVQVKNTGQMYACKKL----DKKRLKKksgekMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHtilDDLELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApGEVY 158
Cdd:cd05607   85 NG---GDLKYHiynvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE-GKPI 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578809600 159 TDYVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05607  161 TQRAGTNGYMAPEILK-EESYSYPVDWFAMGCSIYEMVAGRTPF 203
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1-287 2.03e-20

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 91.15  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMR-EIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14187    6 RRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSmEIAIHRSLAHQHVVGFHGFFEDNDFVYVV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd14187   86 LELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLYHIMMCLGNLIPRHqelfnKNPVFAGvr 239
Cdd:cd14187  166 TLCGTPNYIAPEVL-SKKGHSFEVDIWSIGCIMYTLLVGKPPFE-TSCLKETYLRIKKNEYSIPKH-----INPVAAS-- 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 240 lpeikereplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14187  237 -----------------------LIQKMLQTDPTARPTINELLNDEFF 261
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
1-224 2.18e-20

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 92.79  E-value: 2.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVA---IKKFLESDDDKMvkKIAMREIKLLKQLR-HENLVNLLEVCKKKKRW 76
Cdd:cd05618   19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAmkvVKKELVNDDEDI--DWVQTEKHVFEQASnHPFLVGLHSCFQTESRL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd05618   97 FFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGD 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 157 VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLF--------PGDSDIDQLYHIMMCLGNLIPR 224
Cdd:cd05618  177 TTSTFCGTPNYIAPEILRGE-DYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDYLFQVILEKQIRIPR 251
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
9-216 2.63e-20

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 90.75  E-value: 2.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK--KFLESDDDKMVkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD-- 84
Cdd:cd14190   11 VLGGGKFGKVHTCTEKRTGLKLAAKviNKQNSKDKEMV----LLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEgg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 ---HTILDDlelfpnglDYQVVQK----YLFQIINGIGFCHSHNIIHRDIKPENIL-VSQSG-VVKLCDFGFARTLaAPG 155
Cdd:cd14190   87 elfERIVDE--------DYHLTEVdamvFVRQICEGIQFMHQMRVLHLDLKPENILcVNRTGhQVKIIDFGLARRY-NPR 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 156 EVYTDYVATRWYRAPELLVGD-VKYgkAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMM 216
Cdd:cd14190  158 EKLKVNFGTPEFLSPEVVNYDqVSF--PTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLM 217
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
4-202 2.89e-20

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 92.00  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIK-----KFLESDDDKMVkkIAMREIkLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKvlqkkAILKKKEEKHI--MSERNV-LLKNVKHPFLVGLHFSFQTTDKLYF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVD------HTILDDLELFPNGldyqvvQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd05602   86 VLDYINggelfyHLQRERCFLEPRA------RFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENI 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05602  160 EPNGTTSTFCGTPEYLAPEVLHKQ-PYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-244 3.04e-20

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 90.21  E-value: 3.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDddKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd14662    1 RYELVKDIGSGNFGVARLMRNKETKELVAVK-YIERG--LKIDENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTilddlELFPN----GLDYQVVQKYLF-QIINGIGFCHSHNIIHRDIKPENILV--SQSGVVKLCDFGFARTLAAPG 155
Cdd:cd14662   78 AAGG-----ELFERicnaGRFSEDEARYFFqQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDyVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSD-----------------IDQLYHIMMCL 218
Cdd:cd14662  153 QPKST-VGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDpknfrktiqrimsvqykIPDYVRVSQDC 231
                        250       260
                 ....*....|....*....|....*.
gi 578809600 219 GNLIPRhqeLFNKNPVfAGVRLPEIK 244
Cdd:cd14662  232 RHLLSR---IFVANPA-KRITIPEIK 253
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
9-217 3.11e-20

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 90.36  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK--KFLESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14193   11 ILGGGRFGQVHKCEEKSSGLKLAAKiiKARSQKEKEEVKN----EIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ilddlELFPNGLD--YQVVQ----KYLFQIINGIGFCHSHNIIHRDIKPENILV--SQSGVVKLCDFGFARTLaAPGEVY 158
Cdd:cd14193   87 -----ELFDRIIDenYNLTEldtiLFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRY-KPREKL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVGD-VKYgkAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC 217
Cdd:cd14193  161 RVNFGTPEFLAPEVVNYEfVSF--PTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILAC 218
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
7-216 3.69e-20

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 91.60  E-value: 3.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESD----DDKMvkKIAMREIKLLKQLRHENLVNLLEVC-KKKKRWYLVFE 81
Cdd:cd05615   15 LMVLGKGSFGKVMLAERKGSDELYAIK-ILKKDvviqDDDV--ECTMVEKRVLALQDKPPFLTQLHSCfQTVDRLYFVME 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVdhtilddlelfpNGLD--YQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd05615   92 YV------------NGGDlmYHIQQVgkfkepqavfYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 150 TLAAPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDsDIDQLYHIMM 216
Cdd:cd05615  160 EHMVEGVTTRTFCGTPDYIAPEIIAYQ-PYGRSVDWWAYGVLLYEMLAGQPPFDGE-DEDELFQSIM 224
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1-224 3.70e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 92.07  E-value: 3.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIA--MREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd05593   14 MNDFDYLKLLGKGTFGKVILVREKASGKYYAMK-ILKKEVIIAKDEVAhtLTESRVLKNTRHPFLTSLKYSFQTKDRLCF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTilddlELFPNGLDYQVVQK-----YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd05593   93 VMEYVNGG-----ELFFHLSRERVFSEdrtrfYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 154 PGEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGE-PLFpgDSDIDQLYHIMMCLGNLIPR 224
Cdd:cd05593  168 DAATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFY--NQDHEKLFELILMEDIKFPR 236
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
10-275 4.85e-20

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 89.69  E-value: 4.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMvkKIAMREIKLLKQLR-HENLVNLLEVckkkkrwylVFEFVDHTIL 88
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALK-FVPKPSTKL--KDFLREYNISLELSvHPHIIKTYDV---------AFETEDYYVF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 --------DDLELFP--NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV--SQSGVVKLCDFGFARTLAAPge 156
Cdd:cd13987   69 aqeyapygDLFSIIPpqVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTRRVGST-- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 vytdyVATRW----YRAPELLVGDVKYGKAV----DVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclgnlipRHQEl 228
Cdd:cd13987  147 -----VKRVSgtipYTAPEVCEAKKNEGFVVdpsiDVWAFGVLLFCCLTGNFPWEKADSDDQFYEEFV-------RWQK- 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 229 fNKNPVfagvrLPeikerePLERRypkLSEVVIDLAKKCLHIDPDKR 275
Cdd:cd13987  214 -RKNTA-----VP------SQWRR---FTPKALRMFKKLLAPEPERR 245
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
9-251 5.22e-20

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 90.77  E-value: 5.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLES----DDDKmvkKIAMREIKLLKqLRHEN--LVNLLEVCKKKKRWYLVFEF 82
Cdd:cd05620    2 VLGKGSFGKVLLAELKGKGEYFAVKALKKDvvliDDDV---ECTMVEKRVLA-LAWENpfLTHLYCTFQTKEHLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VdhtilddlelfpNGLD--YQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd05620   78 L------------NGGDlmFHIQDKgrfdlyratfYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 151 LAAPGEVYTDYVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDsDIDQLYHIMMCLGNLIPRHQELFN 230
Cdd:cd05620  146 NVFGDNRASTFCGTPDYIAPEILQG-LKYTFSVDWWSFGVLLYEMLIGQSPFHGD-DEDELFESIRVDTPHYPRWITKES 223
                        250       260
                 ....*....|....*....|.
gi 578809600 231 KNpvfagvRLPEIKEREPLER 251
Cdd:cd05620  224 KD------ILEKLFERDPTRR 238
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
3-196 5.63e-20

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 90.26  E-value: 5.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNL---------------L 67
Cdd:cd14049    7 EFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYhtawmehvqlmlyiqM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  68 EVCKKKKRWYLVfefvDHTILDDLELFPNGL----DYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV-VKL 142
Cdd:cd14049   87 QLCELSLWDWIV----ERNKRPCEEEFKSAPytpvDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIhVRI 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 143 CDFGFA------------RTLAAPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd14049  163 GDFGLAcpdilqdgndstTMSRLNGLTHTSGVGTCLYAAPEQLEGS-HYDFKSDMYSIGVILLELF 227
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-290 6.35e-20

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 89.33  E-value: 6.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMK--CRNKDTGRI-VAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVD-- 84
Cdd:cd05060    3 LGHGNFGSVRKgvYLMKSGKEVeVAVK-TLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPlg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 --HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYV 162
Cdd:cd05060   81 plLKYLKKRREIPV----SDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDYYRATT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRW---YRAPELlvgdVKYGK---AVDVWAIGCLVTEMF-MGEPLFPGDSDIDqlyhIMMCLGNliprhqelfnknpvf 235
Cdd:cd05060  157 AGRWplkWYAPEC----INYGKfssKSDVWSYGVTLWEAFsYGAKPYGEMKGPE----VIAMLES--------------- 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 236 aGVRLPeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELlhHDFFQMD 290
Cdd:cd05060  214 -GERLP----------RPEECPQEIYSIMLSCWKYRPEDRPTFSEL--ESTFRRD 255
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
10-196 8.12e-20

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 89.24  E-value: 8.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMK--CRNKDTgriVAIKKFLESdddKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd05112   12 IGSGQFGLVHLgyWLNKDK---VAIKTIREG---AMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRW 166
Cdd:cd05112   86 LSDYLRTQRGlFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVL--DDQYTSSTGTKF 163
                        170       180       190
                 ....*....|....*....|....*....|...
gi 578809600 167 ---YRAPELLVGDvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05112  164 pvkWSSPEVFSFS-RYSSKSDVWSFGVLMWEVF 195
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
3-286 8.38e-20

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 89.69  E-value: 8.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIK-KFLE---SDDDKMV-KKIAMREIKLLKQLRHENLVNLlevckkkkrwY 77
Cdd:cd13990    1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKiHQLNkdwSEEKKQNyIKHALREYEIHKSLDHPRIVKL----------Y 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLELFP-NGLDYQVVQK----------YLFQIINGIGFCHSHN--IIHRDIKPENILV---SQSGVVK 141
Cdd:cd13990   71 DVFEIDTDSFCTVLEYCDgNDLDFYLKQHksiperearsIIMQVVSALKYLNEIKppIIHYDLKPGNILLhsgNVSGEIK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 142 LCDFGFARTLaaPGEVYTDY--------VATRWYRAPELLV---GDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidq 210
Cdd:cd13990  151 ITDFGLSKIM--DDESYNSDgmeltsqgAGTYWYLPPECFVvgkTPPKISSKVDVWSVGVIFYQMLYGRKPF-------- 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 211 lyhimmclGNLIPRHQELFNKNPvfagvrlpeIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd13990  221 --------GHNQSQEAILEENTI---------LKATEVEFPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
9-281 9.75e-20

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 88.91  E-value: 9.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRiVAIKKFLEsDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TI 87
Cdd:cd05085    3 LLGKGNFGEVYKGTLKDKTP-VAVKTCKE-DLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGgDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlaAPGEVYTD----YVA 163
Cdd:cd05085   81 LSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ--EDDGVYSSsglkQIP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRWyRAPELLvGDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGdsdidqlyhimmclgnliprhqelfnknpvfagvrLPE 242
Cdd:cd05085  159 IKW-TAPEAL-NYGRYSSESDVWSFGILLWETFsLGVCPYPG-----------------------------------MTN 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578809600 243 IKEREPLERRY-----PKLSEVVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd05085  202 QQAREQVEKGYrmsapQRCPEDIYKIMQRCWDYNPENRPKFSEL 245
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
10-205 1.14e-19

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 89.32  E-value: 1.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESD-DDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd08229   32 IGRGQFSEVYRATCLLDGVPVALKKVQIFDlMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDL--------ELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD 160
Cdd:cd08229  112 SRMikhfkkqkRLIPE----KTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHS 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 161 YVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGD 205
Cdd:cd08229  188 LVGTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
9-287 1.33e-19

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 89.68  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKKIAM------REIklLKQLRHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd05601    8 VIGRGHFGEVQVVKEKATGDIYAMKVLKKSE---TLAQEEVsffeeeRDI--MAKANSPWITKLQYAFQDSENLYLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 vdHTILDDLEL---FPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd05601   83 --HPGGDLLSLlsrYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DY-VATRWYRAPELLV---GDVK--YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnlipRHQELFnknp 233
Cdd:cd05601  161 KMpVGTPDYIAPEVLTsmnGGSKgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIM--------NFKKFL---- 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 234 vfagvRLPEikereplerrYPKLSEVVIDLAKKCLhIDPDKRPFCAELLHHDFF 287
Cdd:cd05601  229 -----KFPE----------DPKVSESAVDLIKGLL-TDAKERLGYEGLCCHPFF 266
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
10-282 1.39e-19

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 90.06  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKC-----RNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHE-NLVNLL--------------EV 69
Cdd:cd14207   15 LGRGAFGKVVQAsafgiKKSPTCRVVAVKMLKEGATASEYKAL-MTELKILIHIGHHlNVVNLLgactksggplmvivEY 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  70 CK--------KKKRWYLVFE---------------------------------------FVDHTILDDLE--------LF 94
Cdd:cd14207   94 CKygnlsnylKSKRDFFVTNkdtslqeelikekkeaeptggkkkrlesvtssesfassgFQEDKSLSDVEeeeedsgdFY 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  95 PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaapgEVYT--DYV-------ATR 165
Cdd:cd14207  174 KRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLAR------DIYKnpDYVrkgdarlPLK 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 166 WYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDqlyhimmclgnliprhQELFNKnpVFAGVRLpeik 244
Cdd:cd14207  248 WM-APESIF-DKIYSTKSDVWSYGVLLWEIFsLGASPYPG-VQID----------------EDFCSK--LKEGIRM---- 302
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 578809600 245 eREPlERRYPKLSEVVIDlakkCLHIDPDKRPFCAELL 282
Cdd:cd14207  303 -RAP-EFATSEIYQIMLD----CWQGDPNERPRFSELV 334
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
10-285 1.44e-19

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 89.64  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR-------NKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd05099   20 LGEGCFGQVVRAEaygidksRPDQTVTVAVKMLKDNATDKDLADL-ISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDL--ELFPNGLDY----------QVVQKYL----FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd05099   99 YAAKGNLREFlrARRPPGPDYtfditkvpeeQLSFKDLvscaYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADF 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARtlaapGEVYTDY--------VATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGdsdidqlyhimm 216
Cdd:cd05099  179 GLAR-----GVHDIDYykktsngrLPVKWM-APEALFDRV-YTHQSDVWSFGILMWEIFtLGGSPYPG------------ 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 217 clgnlIPrHQELFNKnpvfagvrlpeIKEREPLERRYPKLSEVVIdLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd05099  240 -----IP-VEELFKL-----------LREGHRMDKPSNCTHELYM-LMRECWHAVPTQRPTFKQLVEAL 290
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
9-288 1.55e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIaMREIKLLKQLR-HENLVNLLEVCKKKKRWYLVFE-FVDHT 86
Cdd:cd14174    9 LLGEGAYAKVQGCVSLQNGKEYAVK-IIEKNAGHSRSRV-FREVETLYQCQgNKNILELIEFFEDDTRFYLVFEkLRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFAR---------TLAAP 154
Cdd:cd14174   87 ILAHIQKRKH-FNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCEspdKVSPVKICDFDLGSgvklnsactPITTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 gEVYTDyVATRWYRAPELLVGDVK----YGKAVDVWAIGCLVTEMFMGEPLFPG----DSDIDQLYHIMMCLGNLIPRHQ 226
Cdd:cd14174  166 -ELTTP-CGSAEYMAPEVVEVFTDeatfYDKRCDLWSLGVILYIMLSGYPPFVGhcgtDCGWDRGEVCRVCQNKLFESIQ 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 227 ElfnknpvfagvrlpeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14174  244 E----------------GKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
10-287 1.78e-19

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 88.14  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAikkFLESDDDKMVKKIAMR---EIKLLKQLRHENLVNLLEVCKKKKRWY----LVFEF 82
Cdd:cd14033    9 IGRGSFKTVYRGLDTETTVEVA---WCELQTRKLSKGERQRfseEVEMLKGLQHPNIVRFYDSWKSTVRGHkciiLVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVS-QSGVVKLCDFGFARTLAApgEVYT 159
Cdd:cd14033   86 MTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATLKRA--SFAK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLvgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYhimmclgnlipRHQELFNKNPVFAGVR 239
Cdd:cd14033  164 SVIGTPEFMAPEMY--EEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIY-----------RKVTSGIKPDSFYKVK 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 240 LPEIKEreplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14033  231 VPELKE-----------------IIEGCIRTDKDERFTIQDLLEHRFF 261
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-282 1.97e-19

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 87.79  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKFleSDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd05039   13 LIGKGEFGDVMLGDYR--GQKVAVKCL--KDDSTAAQAF-LAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 ddlelfpngLDY------QVVQK-----YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlAAPGEV 157
Cdd:cd05039   88 ---------VDYlrsrgrAVITRkdqlgFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK--EASSNQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 158 YTDYVATRWyRAPELLvGDVKYGKAVDVWAIGCLVTEMF-MGEPLFPgdsdidqlyhiMMCLGNLIPRhqelfnknpVFA 236
Cdd:cd05039  157 DGGKLPIKW-TAPEAL-REKKFSTKSDVWSFGILLWEIYsFGRVPYP-----------RIPLKDVVPH---------VEK 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 237 GVRLpEIKEREPLErrypklsevVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd05039  215 GYRM-EAPEGCPPE---------VYKVMKNCWELDPAKRPTFKQLR 250
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
10-196 2.06e-19

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 88.29  E-value: 2.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVM--KCRNKDTGR---IVAIKKFLESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05049   13 LGEGAFGKVFlgECYNLEPEQdkmLVAVKTLKDASSPD-ARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYME 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLeLFPNGLDYQVVQKY---------------LFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd05049   92 HGDLNKF-LRSHGPDAAFLASEdsapgeltlsqllhiAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMSR 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 150 tlaapgEVY-TDY--------VATRWYrAPEllvgDVKYGKAV---DVWAIGCLVTEMF 196
Cdd:cd05049  171 ------DIYsTDYyrvgghtmLPIRWM-PPE----SILYRKFTtesDVWSFGVVLWEIF 218
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
9-288 2.20e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 88.88  E-value: 2.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFefv 83
Cdd:cd05632    9 VLGKGGFGEVCACQVRATGKMYACKRL----EKKRIKKrkgesMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 dhTILD--DLELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApGE 156
Cdd:cd05632   82 --TIMNggDLKFHiynmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPE-GE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhqelfnknpvfa 236
Cdd:cd05632  159 SIRGRVGTVGYMAPEVL-NNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKE----------------------------- 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 237 GVRLPEIKER--EPLERRYPKLSEVVIDLAKKCLHIDPDKRPFC-----AELLHHDFFQ 288
Cdd:cd05632  209 KVKREEVDRRvlETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCqeegaGEVKRHPFFR 267
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-195 2.96e-19

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 88.01  E-value: 2.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKK--KRW----- 76
Cdd:cd14048    8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAREKV-LREVRALAKLDHPGIVRYFNAWLERppEGWqekmd 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 ----YLVFEFVDHTILDDL---ELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA- 148
Cdd:cd14048   87 evylYIQMQLCRKENLKDWmnrRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVt 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 149 --------RTLAAPGEVY---TDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEM 195
Cdd:cd14048  167 amdqgepeQTVLTPMPAYakhTGQVGTRLYMSPEQIHGN-QYSEKVDIFALGLILFEL 223
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
2-230 3.25e-19

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 88.94  E-value: 3.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKKiamREIKLLKQLRhENLVNllevckKKKRW----- 76
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWE---MLKR---AETACFREER-DVLVN------GDRRWitklh 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 ---------YLVFEF-VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd05597   68 yafqdenylYLVMDYyCGGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTLAAPGEVYTDY-VATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnl 221
Cdd:cd05597  148 SCLKLREDGTVQSSVaVGTPDYISPEILQamedGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM------ 221

                 ....*....
gi 578809600 222 ipRHQELFN 230
Cdd:cd05597  222 --NHKEHFS 228
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-215 3.45e-19

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 89.68  E-value: 3.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHEN-LVNLLEVCKKKKRWYLVF 80
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPwVVQLFYAFQDDRYLYMVM 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTilDDLELFPNgldYQVVQK----YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd05622  153 EYMPGG--DLVNLMSN---YDVPEKwarfYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGM 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 157 VYTDY-VATRWYRAPELLV---GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM 215
Cdd:cd05622  228 VRCDTaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 290
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
11-196 3.46e-19

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 87.82  E-value: 3.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCR-----NKDTGRIVAIKKFLESDDDKmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05048   14 GEGAFGKVYKGEllgpsSEESAISVAIKTLKENASPK-TQQDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMAH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TIL----------------DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd05048   93 GDLheflvrhsphsdvgvsSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLSR 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 150 tlaapgEVYT-DY--------VATRWYrAPELLVgdvkYGK---AVDVWAIGCLVTEMF 196
Cdd:cd05048  173 ------DIYSsDYyrvqskslLPVRWM-PPEAIL----YGKfttESDVWSFGVVLWEIF 220
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
10-283 4.38e-19

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 87.12  E-value: 4.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DL-ELFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFAR----TLAAPGEVYTDYV 162
Cdd:cd13978   81 SLlEREIQDVPWSLRFRIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKlgmkSISANRRRGTENL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 A-TRWYRAPELLvgDVKYGK---AVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprhqelfnknpVFAGV 238
Cdd:cd13978  161 GgTPIYMAPEAF--DDFNKKptsKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQI-------------------VSKGD 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 239 RlPEIKErEPLERRYPKLSEvVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd13978  220 R-PSLDD-IGRLKQIENVQE-LISLMIRCWDGNPDARPTFLECLD 261
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
9-224 4.63e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 88.44  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLES----DDDKMVKKIAMREIKLlkQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05619   12 MLGKGSFGKVFLAELKGTNQFFAIKALKKDvvlmDDDVECTMVEKRVLSL--AWEHPFLTHLFCTFQTKENLFFVMEYLN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTlAAPGEVYTD-YVA 163
Cdd:cd05619   90 GGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKE-NMLGDAKTStFCG 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 164 TRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGdSDIDQLYHIMMCLGNLIPR 224
Cdd:cd05619  169 TPDYIAPEILLGQ-KYNTSVDWWSFGVLLYEMLIGQSPFHG-QDEEELFQSIRMDNPFYPR 227
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
10-276 6.10e-19

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 86.52  E-value: 6.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHtilD 89
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKAKFLQ-EARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQG---G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVVQKYLFQIIN----GIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-----TLAAPGEVytD 160
Cdd:cd05084   80 DFLTFLRTEGPRLKVKELIRMVEnaaaGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSReeedgVYAATGGM--K 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWyRAPELL-VGdvKYGKAVDVWAIGCLVTEMF-MGEPLFPgdsdidqlyhimmclgnlIPRHQElfNKNPVFAGV 238
Cdd:cd05084  158 QIPVKW-TAPEALnYG--RYSSESDVWSFGILLWETFsLGAVPYA------------------NLSNQQ--TREAVEQGV 214
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 578809600 239 RLPeIKEREPlerrypklsEVVIDLAKKCLHIDPDKRP 276
Cdd:cd05084  215 RLP-CPENCP---------DEVYRLMEQCWEYDPRKRP 242
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
2-215 6.39e-19

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 88.52  E-value: 6.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK---KFlesdddKMVKK----IAMREIKLLKQLRHENLVNLLEVCKKKK 74
Cdd:cd05621   52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKllsKF------EMIKRsdsaFFWEERDIMAFANSPWVVQLFCAFQDDK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVDHTilDDLELFPNgldYQVVQK----YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd05621  126 YLYMVMEYMPGG--DLVNLMSN---YDVPEKwakfYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMK 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 151 LAAPGEVYTDY-VATRWYRAPELLV---GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM 215
Cdd:cd05621  201 MDETGMVHCDTaVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIM 269
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
9-202 8.21e-19

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 86.62  E-value: 8.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesdDDKMVKK-----IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05630    7 VLGKGGFGEVCACQVRATGKMYACKKL----EKKRIKKrkgeaMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHtilDDLELF-----PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApGEVY 158
Cdd:cd05630   83 NG---GDLKFHiyhmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPE-GQTI 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578809600 159 TDYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05630  159 KGRVGTVGYMAPE-VVKNERYTFSPDWWALGCLLYEMIAGQSPF 201
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
2-286 8.44e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 86.99  E-value: 8.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESdddkmvKKIAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd14177    4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKS------KRDPSEEIEILMRYgQHPNIITLKDVYDDGRYVYLVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV----SQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd14177   78 ELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGENG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG-EPLFPGDSDIDQlyHIMMCLGNliprhqelfNKNPVF 235
Cdd:cd14177  158 LLLTPCYTANFVAPEVLMRQ-GYDAACDIWSLGVLLYTMLAGyTPFANGPNDTPE--EILLRIGS---------GKFSLS 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 236 AGvrlpeikereplerRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14177  226 GG--------------NWDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHSW 262
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
8-206 9.05e-19

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 87.03  E-value: 9.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   8 GLVGEGSYGMVMKcrNKDTGRIVAIKKFLESDDDKMVkkiAMREIKLLKQLRHENLVNLLEVCKK-----KKRWYLVFEF 82
Cdd:cd14054    1 QLIGQGRYGTVWK--GSLDERPVAVKVFPARHRQNFQ---NEKDIYELPLMEHSNILRFIGADERptadgRMEYLLVLEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSH---------NIIHRDIKPENILVSQSGVVKLCDFGFARTLAA 153
Cdd:cd14054   76 APKGSLCSY-LRENTLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRG 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDY----------VATRWYRAPELLVGDVK------YGKAVDVWAIGCLVTEMFMG-EPLFPGDS 206
Cdd:cd14054  155 SSLVRGRPgaaenasiseVGTLRYMAPEVLEGAVNlrdcesALKQVDVYALGLVLWEIAMRcSDLYPGES 224
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
10-214 9.52e-19

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 87.16  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKF-----LESDDdkmvkkIAMREIKLLKQLRHENLVNLL--EVCKKKKRWYLVFEF 82
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFnnlsfMRPLD------VQMREFEVLKKLNHKNIVKLFaiEEELTTRHKVLVMEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VD----HTILDDLElfpN--GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL--VSQSG--VVKLCDFGFARTLa 152
Cdd:cd13988   75 CPcgslYTVLEEPS---NayGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGqsVYKLTDFGAAREL- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDV-------KYGKAVDVWAIGC----LVTEMFMGEPLFPGDSDIDQLYHI 214
Cdd:cd13988  151 EDDEQFVSLYGTEEYLHPDMYERAVlrkdhqkKYGATVDLWSIGVtfyhAATGSLPFRPFEGPRRNKEVMYKI 223
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2-229 1.01e-18

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 88.53  E-value: 1.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIK-LLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERnVLVNGDCQWITTLHYAFQDENYLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EF-VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd05624  152 DYyVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNDDGTVQS 231
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 160 DY-VATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnlipRHQELF 229
Cdd:cd05624  232 SVaVGTPDYISPEILQamedGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM--------NHEERF 298
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
2-206 1.02e-18

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 87.41  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAiKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMA-RKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFC-HSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTD 160
Cdd:cd06649   84 HMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI--DSMANS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 161 YVATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGE-PLFPGDS 206
Cdd:cd06649  162 FVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVELAIGRyPIPPPDA 207
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
1-224 1.03e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 87.77  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVA---IKKFLESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVC-KKKKRW 76
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAmkvVKKELVHDDEDI--DWVQTEKHVFEQASSNPFLVGLHSCfQTTSRL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd05617   92 FLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGD 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 157 VYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLF------PGDSDIDQLYHIMMCLGNLIPR 224
Cdd:cd05617  172 TTSTFCGTPNYIAPEILRGE-EYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVILEKPIRIPR 244
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
24-288 1.29e-18

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 86.22  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  24 KDTGRIVAI----KKFLE---SDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKK-KKRWYLVFEFVDHTIL------D 89
Cdd:cd14011   18 KSTKQEVSVfvfeKKQLEeysKRDREQILELLKRGVKQLTRLRHPRILTVQHPLEEsRESLAFATEPVFASLAnvlgerD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLD----YQVVQKY-LFQIINGIGFCHSH-NIIHRDIKPENILVSQSGVVKLCDFGFArtLAAPGEVYTDYVA 163
Cdd:cd14011   98 NMPSPPPELQdyklYDVEIKYgLLQISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFC--ISSEQATDQFPYF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 164 TRW-------------YRAPElLVGDVKYGKAVDVWAIGCLVTEMFM-GEPLFpgdsdidqlyhimMCLGNLIPrhqelF 229
Cdd:cd14011  176 REYdpnlpplaqpnlnYLAPE-YILSKTCDPASDMFSLGVLIYAIYNkGKPLF-------------DCVNNLLS-----Y 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 230 NKNPVFAGVRLPEIKEREPLERRypklsevviDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14011  237 KKNSNQLRQLSLSLLEKVPEELR---------DHVKTLLNVTPEVRPDAEQLSKIPFFD 286
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
10-275 1.30e-18

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 86.16  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK----------------------KFLESDDDKMVKKI--AMREIKLLKQLRHENLVN 65
Cdd:cd14200    8 IGKGSYGVVKLAYNESDDKYYAMKvlskkkllkqygfprrppprgsKAAQGEQAKPLAPLerVYQEIAILKKLDHVNIVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  66 LLEVCKK--KKRWYLVFEFVDHTILDDLelfPNGLDYQVVQK--YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVK 141
Cdd:cd14200   88 LIEVLDDpaEDNLYMVFDLLRKGPVMEV---PSDKPFSEDQArlYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 142 LCDFGFARTLAAPGEVYTDYVATRWYRAPELLV--GDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdIDQLyhimmclg 219
Cdd:cd14200  165 IADFGVSNQFEGNDALLSSTAGTPAFMAPETLSdsGQSFSGKALDVWAMGVTLYCFVYGKCPF-----IDEF-------- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 220 nLIPRHQELFNKNPVFagvrlPEikereplerrYPKLSEVVIDLAKKCLHIDPDKR 275
Cdd:cd14200  232 -ILALHNKIKNKPVEF-----PE----------EPEISEELKDLILKMLDKNPETR 271
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1-283 1.51e-18

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 85.86  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMK-----CRNKDTGRIVAIKKFleSDDDKMVKKIA-MREIKLLKQLRHENLVNLLEVCKKKK 74
Cdd:cd05032    5 REKITLIRELGQGSFGMVYEglakgVVKGEPETRVAIKTV--NENASMRERIEfLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVDHTILDDL-------ELFPNGLDYQVVQKYL---FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCD 144
Cdd:cd05032   83 PTLVVMELMAKGDLKSYlrsrrpeAENNPGLGPPTLQKFIqmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 145 FGFARTLaapgeVYTDY--------VATRWYrAPELLvGDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSdidqlyhim 215
Cdd:cd05032  163 FGMTRDI-----YETDYyrkggkglLPVRWM-APESL-KDGVFTTKSDVWSFGVVLWEMAtLAEQPYQGLS--------- 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 216 mclgnliprHQELFNKnpVFAG--VRLPEikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd05032  227 ---------NEEVLKF--VIDGghLDLPE------------NCPDKLLELMRMCWQYNPKMRPTFLEIVS 273
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
11-197 1.62e-18

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 86.24  E-value: 1.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCR----------------NKDTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKK 74
Cdd:cd05051   14 GEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKM-LRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFV----------DHTILDDLELFPNG--LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKL 142
Cdd:cd05051   93 PLCMIVEYMengdlnqflqKHEAETQGASATNSktLSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKI 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 143 CDFGFARTLaapgevYT-DY--------VATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMFM 197
Cdd:cd05051  173 ADFGMSRNL------YSgDYyriegravLPIRWMAWESILLG--KFTTKSDVWAFGVTLWEILT 228
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
9-234 1.81e-18

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 86.32  E-value: 1.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVA---IKKFLESDDD--------KMVKKIAMReikllkqlrHENLVNLLEVCKKKKRWY 77
Cdd:cd05588    2 VIGRGSYAKVLMVELKKTKRIYAmkvIKKELVNDDEdidwvqteKHVFETASN---------HPFLVGLHSCFQTESRLF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVdhtilddlelfpNGLD--YQVVQK----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd05588   73 FVIEFV------------NGGDlmFHMQRQrrlpeeharfYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDY 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARTLAAPGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLF--------PGDSDIDQLYHIMMC 217
Cdd:cd05588  141 GMCKEGLRPGDTTSTFCGTPNYIAPEILRGE-DYGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDYLFQVILE 219
                        250       260
                 ....*....|....*....|....*.
gi 578809600 218 LGNLIPRH---------QELFNKNPV 234
Cdd:cd05588  220 KPIRIPRSlsvkaasvlKGFLNKNPA 245
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
9-286 1.87e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 85.02  E-value: 1.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesDDDKMVK--------KIAMrEIKLLKQLRH--ENLVNLLEVCKKKKRWYL 78
Cdd:cd14100    7 LLGSGGFGSVYSGIRVADGAPVAIKHV---EKDRVSEwgelpngtRVPM-EIVLLKKVGSgfRGVIRLLDWFERPDSFVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDhtILDDLELF---PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS-QSGVVKLCDFGFARTLAap 154
Cdd:cd14100   83 VLERPE--PVQDLFDFiteRGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLK-- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnlIPRHQELFNKnpv 234
Cdd:cd14100  159 DTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE--------------IIRGQVFFRQ--- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 235 fagvrlpeikereplerrypKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDF 286
Cdd:cd14100  222 --------------------RVSSECQHLIKWCLALRPSDRPSFEDIQNHPW 253
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
10-287 2.07e-18

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 86.86  E-value: 2.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESD--DDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADmiNKNMVHQV-QAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR----------------TL 151
Cdd:cd05610   91 VKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnrelnmmdilttpSM 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAPGEVY-------------------TDY------------------VATRWYRAPELLVGDvKYGKAVDVWAIGCLVTE 194
Cdd:cd05610  171 AKPKNDYsrtpgqvlslisslgfntpTPYrtpksvrrgaarvegeriLGTPDYLAPELLLGK-PHGPAVDWWALGVCLFE 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 195 MFMGEPLFpGDSDIDQLYhimmclgnliprhQELFNKNpvfagVRLPEIKEreplerrypKLSEVVIDLAKKCLHIDPDK 274
Cdd:cd05610  250 FLTGIPPF-NDETPQQVF-------------QNILNRD-----IPWPEGEE---------ELSVNAQNAIEILLTMDPTK 301
                        330
                 ....*....|...
gi 578809600 275 RPFCAELLHHDFF 287
Cdd:cd05610  302 RAGLKELKQHPLF 314
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-208 2.27e-18

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 84.62  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLE---SDDDKMVKKIAMREIKLLKQL--RHENLVNLLEVCKKKKRWYL 78
Cdd:cd14102    2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKervTEWGTLNGVMVPLEIVLLKKVgsGFRGVIKLLDWYERPDGFLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDhtILDDLELF---PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS-QSGVVKLCDFGFARTLAap 154
Cdd:cd14102   82 VMERPE--PVKDLFDFiteKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLK-- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 155 GEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDI 208
Cdd:cd14102  158 DTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEI 211
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
2-229 2.45e-18

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 87.38  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIK-LLKQLRHENLVNLLEVCKKKKRWYLVF 80
Cdd:cd05623   72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERdVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EF-VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd05623  152 DYyVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLKLMEDGTVQS 231
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 160 DY-VATRWYRAPELLV----GDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMmclgnlipRHQELF 229
Cdd:cd05623  232 SVaVGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM--------NHKERF 298
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
11-288 3.01e-18

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 84.75  E-value: 3.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYG---MVMKCRNKDTGRIVAIKkflesdddkMVKKIA-----------MREIKLLKQLRHEN-LVNLLEVCKKKKR 75
Cdd:cd05583    3 GTGAYGkvfLVRKVGGHDAGKLYAMK---------VLKKATivqkaktaehtMTERQVLEAVRQSPfLVTLHYAFQTDAK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVD----HTILDDLELFpnglDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL 151
Cdd:cd05583   74 LHLILDYVNggelFTHLYQREHF----TESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 AAP-GEVYTDYVATRWYRAPELL-VGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnliprHQELF 229
Cdd:cd05583  150 LPGeNDRAYSFCGTIEYMAPEVVrGGSDGHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEI----------SKRIL 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 230 NKNPVFAgvrlpeikereplerryPKLSEVVIDLAKKCLHIDPDKRPFCA-----ELLHHDFFQ 288
Cdd:cd05583  220 KSHPPIP-----------------KTFSAEAKDFILKLLEKDPKKRLGAGprgahEIKEHPFFK 266
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
10-198 3.26e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 84.97  E-value: 3.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRW-----YLVFEFV 83
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCrLELSVKN--KDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLELFPN---GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLCDFGFARTLAApGEV 157
Cdd:cd14039   79 SGGDLRKLLNKPEnccGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkiVHKIIDLGYAKDLDQ-GSL 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809600 158 YTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG 198
Cdd:cd14039  158 CTSFVGTLQYLAPELFENK-SYTVTVDYWSFGTMVFECIAG 197
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
2-290 3.54e-18

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 85.10  E-value: 3.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIK----KFLESDDDKMVKKIAmreikLLKQLRHENLVNLLEVCKKKKRWY 77
Cdd:cd14168   10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKcipkKALKGKESSIENEIA-----VLRKIKHENIVALEDIYESPNHLY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFARtLAAP 154
Cdd:cd14168   85 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSK-MEGK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclgnliprhqelfnkNPV 234
Cdd:cd14168  164 GDVMSTACGTPGYVAPEVL-AQKPYSKAVDCWSIGVIAYILLCGYPPFYDEND------------------------SKL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 235 FAGVRLPEIKEREPLerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQMD 290
Cdd:cd14168  219 FEQILKADYEFDSPY---WDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGD 271
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
9-288 3.62e-18

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 85.37  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIK---KFLESDDDKMVKKIAMREIklLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05574    8 LLGKGDVGRVYLVRLKGTGKLFAMKvldKEEMIKRNKVKRVLTEREI--LATLDHPFLPTLYASFQTSTHLCFVMDYCPG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TilddlELF------PNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF------------- 145
Cdd:cd05574   86 G-----ELFrllqkqPGKrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 ------GFARTLAAPGEVYT----------DYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDID 209
Cdd:cd05574  161 rkslrkGSRRSSVKSIEKETfvaepsarsnSFVGTEEYIAPEVIKGD-GHGSAVDWWTLGILLYEMLYGTTPFKGSNRDE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 210 QLYHIMmclgnliprhqelfNKNPVFAGvrlpeikereplerrYPKLSEVVIDLAKKCLHIDPDKRPFC----AELLHHD 285
Cdd:cd05574  240 TFSNIL--------------KKELTFPE---------------SPPVSSEAKDLIRKLLVKDPSKRLGSkrgaSEIKRHP 290

                 ...
gi 578809600 286 FFQ 288
Cdd:cd05574  291 FFR 293
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
9-284 3.98e-18

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 84.69  E-value: 3.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIaMREIKLLKQLR-HENLVNLLEVCKKKKRWYLVFE-FVDHT 86
Cdd:cd14173    9 VLGEGAYARVQTCINLITNKEYAVK-IIEKRPGHSRSRV-FREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEkMRGGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFP--NGLDYQVVQKylfQIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFARTLAAPGE---VY 158
Cdd:cd14173   87 ILSHIHRRRhfNELEASVVVQ---DIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKLNSDcspIS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVAT----RWYRAPELLVGDVK----YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHimmcLGNLIPRHQelfn 230
Cdd:cd14173  164 TPELLTpcgsAEYMAPEVVEAFNEeasiYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDCGWD----RGEACPACQ---- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 231 kNPVFAGVRlpEIKEREPlERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14173  236 -NMLFESIQ--EGKYEFP-EKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQH 285
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1-276 4.22e-18

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 84.26  E-value: 4.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKdtGRIVAIKKFleSDDDKMVKKIAmrEIKLLKQLRHENLVNLLEV-CKKKKRWYLV 79
Cdd:cd05082    5 MKELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCI--KNDATAQAFLA--EASVMTQLRHSNLVQLLGViVEEKGGLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDLeLFPNG---LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE 156
Cdd:cd05082   79 TEYMAKGSLVDY-LRSRGrsvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 vyTDYVATRWyRAPELLvGDVKYGKAVDVWAIGCLVTEMF-MGEPLFPgdsdidqlyhiMMCLGNLIPRHQELFNKNPvf 235
Cdd:cd05082  158 --TGKLPVKW-TAPEAL-REKKFSTKSDVWSFGILLWEIYsFGRVPYP-----------RIPLKDVVPRVEKGYKMDA-- 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 578809600 236 agvrlPEikereplerrypKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd05082  221 -----PD------------GCPPAVYDVMKNCWHLDAAMRP 244
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
10-202 4.35e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 85.09  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK---KFLESDddkmvkkiAMREIKLLKQLR-HENLVNLLEVCKKKKRWYLVFEfvdh 85
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNQEYAVKivsKRMEAN--------TQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVME---- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 tILDDLELFPngldyQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFARTLA 152
Cdd:cd14179   83 -LLKGGELLE-----RIKKKQHFseteashimrKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14179  157 PDNQPLKTPCFTLHYAAPELLNYN-GYDESCDLWSLGVILYTMLSGQVPF 205
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
9-290 4.36e-18

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 84.40  E-value: 4.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKC--RNKDTGRI-VAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWyLVFEFVDH 85
Cdd:cd05056   13 CIGEGQFGDVYQGvyMSPENEKIaVAVKTCKNCTSPSVREKF-LQEAYIMRQFDHPHIVKLIGVITENPVW-IVMELAPL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDD-LELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEVYTDYVAT 164
Cdd:cd05056   91 GELRSyLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYM----EDESYYKAS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 R------WYrAPElLVGDVKYGKAVDVWAIGCLVTEMFM-GEPLFPGDSDIDQLYHImmclgnliprhqelfnknpvfag 237
Cdd:cd05056  167 KgklpikWM-APE-SINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRI----------------------- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 238 vrlpEIKEREPLErryPKLSEVVIDLAKKCLHIDPDKRPFCAELLH--HDFFQMD 290
Cdd:cd05056  222 ----ENGERLPMP---PNCPPTLYSLMTKCWAYDPSKRPRFTELKAqlSDILQEE 269
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
9-287 4.86e-18

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 83.91  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAM-REIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd14188    8 VLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIdKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWY 167
Cdd:cd14188   88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTPNY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 168 RAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLFpgdsdidqlyhimmclgnliprhqELFNKNPVFAGVRlpeikere 247
Cdd:cd14188  168 LSPEVL-NKQGHGCESDIWALGCVMYTMLLGRPPF------------------------ETTNLKETYRCIR-------- 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578809600 248 plERRY---PKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:cd14188  215 --EARYslpSSLLAPAKHLIASMLSKNPEDRPSLDEIIRHDFF 255
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
10-282 5.03e-18

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 83.78  E-value: 5.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVM--KCRNKDTGRIVAIKKFLESDDDkmvkkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-T 86
Cdd:cd05113   12 LGTGQFGVVKygKWRGQYDVAIKMIKEGSMSEDE------FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANgC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRW 166
Cdd:cd05113   86 LLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL--DDEYTSSVGSKF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 ---YRAPELLVgDVKYGKAVDVWAIGCLVTEMFmgeplfpgdsdidqlyhimmCLGNLiprHQELFNKNP----VFAGVR 239
Cdd:cd05113  164 pvrWSPPEVLM-YSKFSSKSDVWAFGVLMWEVY--------------------SLGKM---PYERFTNSEtvehVSQGLR 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 578809600 240 LPEikereplerryPKL-SEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd05113  220 LYR-----------PHLaSEKVYTIMYSCWHEKADERPTFKILL 252
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
9-202 5.16e-18

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 83.89  E-value: 5.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDdkmvkkiAMREIKLLKQLRH-ENLVNLLEVCK---KKKRWYLVFefvd 84
Cdd:cd14172   11 VLGLGVNGKVLECFHRRTGQKCALKLLYDSPK-------ARREVEHHWRASGgPHIVHILDVYEnmhHGKRCLLII---- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLELFPN----GlDYQVVQKYLFQIINGIG----FCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAA 153
Cdd:cd14172   80 MECMEGGELFSRiqerG-DQAFTEREASEIMRDIGtaiqYLHSMNIAHRDVKPENLLYTskeKDAVLKLTDFGFAKETTV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 154 PGEVYTDyVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14172  159 QNALQTP-CYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGFPPF 205
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
4-288 5.18e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 84.38  E-value: 5.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESD---DDKMVKKIAMREIKLLKqlrhEN--LVNLLEVCKKKKRWYL 78
Cdd:cd05609    2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNlilRNQIQQVFVERDILTFA----ENpfVVSMYCSFETKRHLCM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVD----HTILDDLELFPngldYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART--LA 152
Cdd:cd05609   78 VMEYVEggdcATLLKNIGPLP----VDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIglMS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDY-------------VATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDidqlyhimmclg 219
Cdd:cd05609  154 LTTNLYEGHiekdtrefldkqvCGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFFGDTP------------ 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 220 nliprhQELFNkNPVFAGVRLPEIKEREPLERRypklsevviDLAKKCLHIDPDKR---PFCAELLHHDFFQ 288
Cdd:cd05609  221 ------EELFG-QVISDEIEWPEGDDALPDDAQ---------DLITRLLQQNPLERlgtGGAEEVKQHPFFQ 276
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
11-215 5.41e-18

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 83.72  E-value: 5.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKkfLESDDDKMvkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDD 90
Cdd:cd14109   13 KRAAQGAPFHVTERSTGRNFLAQ--LRYGDPFL-----MREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  91 LELFPNGLDY---QVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVsQSGVVKLCDFGFARTLAApGEVYTDYVATRWY 167
Cdd:cd14109   86 RDNLLPGKDYyteRQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRRLLR-GKLTTLIYGSPEF 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 168 RAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM 215
Cdd:cd14109  164 VSPE-IVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVR 210
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
10-276 6.58e-18

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 83.94  E-value: 6.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMV-MKCRNKDTGriVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TI 87
Cdd:cd05072   15 LGAGQFGEVwMGYYNNSTK--VAVKTL---KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKgSL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLE-------LFPNGLDYQVvqkylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTD 160
Cdd:cd05072   90 LDFLKsdeggkvLLPKLIDFSA------QIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE--DNEYTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRW---YRAPELlvgdVKYGKAV---DVWAIGCLVTEMFM-GEPLFPGDSDIDqlyhIMMCLGNliprhqelfnknp 233
Cdd:cd05072  162 REGAKFpikWTAPEA----INFGSFTiksDVWSFGILLYEIVTyGKIPYPGMSNSD----VMSALQR------------- 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 578809600 234 vfaGVRLPEIkEREPLErrypklsevVIDLAKKCLHIDPDKRP 276
Cdd:cd05072  221 ---GYRMPRM-ENCPDE---------LYDIMKTCWKEKAEERP 250
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-196 7.04e-18

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 84.26  E-value: 7.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR------------NKDTGR--IVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKR 75
Cdd:cd05097   13 LGEGQFGEVHLCEaeglaeflgegaPEFDGQpvLVAVKM-LRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHtilDDLELF------------PNGLDYQVVQKYLF---QIINGIGFCHSHNIIHRDIKPENILVSQSGVV 140
Cdd:cd05097   92 LCMITEYMEN---GDLNQFlsqreiestfthANNIPSVSIANLLYmavQIASGMKYLASLNFVHRDLATRNCLVGNHYTI 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 141 KLCDFGFARTLAApGEVY----TDYVATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05097  169 KIADFGMSRNLYS-GDYYriqgRAVLPIRWMAWESILLG--KFTTASDVWAFGVTLWEMF 225
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
10-283 7.08e-18

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 83.47  E-value: 7.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEE--TQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLelfPNGLD--YQVVQKYLF--QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL----AAPGEVYTDY 161
Cdd:cd14221   79 GI---IKSMDshYPWSQRVSFakDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdekTQPEGLRSLK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATR----------WYRAPELLVGDvKYGKAVDVWAIGCLVTEMFmgeplfpGDSDIDQLYhimmclgnlIPRHQELFNK 231
Cdd:cd14221  156 KPDRkkrytvvgnpYWMAPEMINGR-SYDEKVDVFSFGIVLCEII-------GRVNADPDY---------LPRTMDFGLN 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 232 NPVFAGVRLPeikereplerryPKLSEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd14221  219 VRGFLDRYCP------------PNCPPSFFPIAVLCCDLDPEKRPSFSKLEH 258
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
10-276 8.47e-18

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 83.80  E-value: 8.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----NKDTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKK--KRWYLVFEFV 83
Cdd:cd05080   12 LGEGHFGKVSLYCydptNDGTGEMVAVKA-LKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQLIMEYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY---TD 160
Cdd:cd05080   91 PLGSLRDY-LPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYrvrED 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 YVATRWYRAPELLvGDVKYGKAVDVWAIGclVTemfmgeplfpgdsdidqLYHIMM-CLGNLIPRHQ--ELFN-KNPVFA 236
Cdd:cd05080  170 GDSPVFWYAPECL-KEYKFYYASDVWSFG--VT-----------------LYELLThCDSSQSPPTKflEMIGiAQGQMT 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578809600 237 GVRLPEIKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd05080  230 VVRLIELLERGERLPCPDKCPQEVYHLMKNCWETEASFRP 269
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1-224 9.76e-18

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 84.70  E-value: 9.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIA--MREIKLLKQLRHENLVNLLEVCKKKKRWYL 78
Cdd:cd05594   24 MNDFEYLKLLGKGTFGKVILVKEKATGRYYAMK-ILKKEVIVAKDEVAhtLTENRVLQNSRHPFLTALKYSFQTHDRLCF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 VFEFVDHTilddlELFPNGLDYQVVQK-----YLFQIINGIGFCHSH-NIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd05594  103 VMEYANGG-----ELFFHLSRERVFSEdrarfYGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578809600 153 APGEVYTDYVATRWYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGE-PLFpgDSDIDQLYHIMMCLGNLIPR 224
Cdd:cd05594  178 KDGATMKTFCGTPEYLAPEVL-EDNDYGRAVDWWGLGVVMYEMMCGRlPFY--NQDHEKLFELILMEEIRFPR 247
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
5-287 1.14e-17

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 83.01  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLV---GEGSYGMV-MKCRNKDTGriVAIKKFLESdddKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVF 80
Cdd:cd05067    7 ETLKLVerlGAGQFGEVwMGYYNGHTK--VAIKSLKQG---SMSPDAFLAEANLMKQLQHQRLVRLYAVVTQEP-IYIIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgeVY 158
Cdd:cd05067   81 EYMENGSLVDFLKTPSGIKLTINKllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLI-----ED 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVA-------TRWyRAPELlvgdVKYGK---AVDVWAIGCLVTEMFMgeplfpgdsdidqlyhimmclgnliprhqel 228
Cdd:cd05067  156 NEYTAregakfpIKW-TAPEA----INYGTftiKSDVWSFGILLTEIVT------------------------------- 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 229 FNKNPvFAGVRLPEIKERepLERRY--PK---LSEVVIDLAKKCLHIDPDKRP---FCAELLhHDFF 287
Cdd:cd05067  200 HGRIP-YPGMTNPEVIQN--LERGYrmPRpdnCPEELYQLMRLCWKERPEDRPtfeYLRSVL-EDFF 262
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
12-191 1.45e-17

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 82.72  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  12 EGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMvkKIAMREIKLLKQLR-HENLVNLLE---VCKKKKRW--YLVFEFVDH 85
Cdd:cd14037   13 EGGFAHVYLVKTSNGGNRAALKRVYVNDEHDL--NVCKREIEIMKRLSgHKNIVGYIDssaNRSGNGVYevLLLMEYCKG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDL--ELFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD- 160
Cdd:cd14037   91 GGVIDLmnQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSATTKILPPQTKQGv 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809600 161 -YVA-------TRWYRAPELLvgDVKYGKAV----DVWAIGCL 191
Cdd:cd14037  171 tYVEedikkytTLQYRAPEMI--DLYRGKPIteksDIWALGCL 211
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
8-276 1.59e-17

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 82.32  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   8 GLVGEGSYGMVMK--CRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDH 85
Cdd:cd05116    1 GELGSGNFGTVKKgyYQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEMAEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATR 165
Cdd:cd05116   80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQTHGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 166 W---YRAPELLvGDVKYGKAVDVWAIGCLVTEMF-MGEPLFPG--DSDIDQLyhimmclgnliprhqelfnknpVFAGVR 239
Cdd:cd05116  160 WpvkWYAPECM-NYYKFSSKSDVWSFGVLMWEAFsYGQKPYKGmkGNEVTQM----------------------IEKGER 216
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 578809600 240 LpEIKEREPLErrypklsevVIDLAKKCLHIDPDKRP 276
Cdd:cd05116  217 M-ECPAGCPPE---------MYDLMKLCWTYDVDERP 243
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
2-234 1.83e-17

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 82.19  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNK--DTGRIVAIKKFLESDDDKMvkkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd14112    3 GRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFEVSDEASE----AVREFESLRTLQHENVQRLIAAFKPSNFAYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHtilDDLELFPNGLDY--QVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS--QSGVVKLCDFGFARTLAAPG 155
Cdd:cd14112   79 MEKLQE---DVFTRFSSNDYYseEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKVSKLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTDyVATRWyRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSD----IDQLYHIMMCLGNLIPRH--QE-- 227
Cdd:cd14112  156 KVPVD-GDTDW-ASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDdeeeTKENVIFVKCRPNLIFVEatQEal 233
                        250
                 ....*....|..
gi 578809600 228 -----LFNKNPV 234
Cdd:cd14112  234 rfatwALKKSPT 245
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
1-215 1.99e-17

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 83.95  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKKIAMREIKLLKQLRHEN----LVNLLEVCKKKKRW 76
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKAD---MLEKEQVAHIRAERDILVEAdgawVVKMFYSFQDKRNL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL--AAP 154
Cdd:cd05627   78 YLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLkkAHR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVY--------TDY-------------------------VATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPL 201
Cdd:cd05627  158 TEFYrnlthnppSDFsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFM-QTGYNKLCDWWSLGVIMYEMLIGYPP 236
                        250
                 ....*....|....
gi 578809600 202 FPGDSDIDQLYHIM 215
Cdd:cd05627  237 FCSETPQETYRKVM 250
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
82-284 2.48e-17

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 83.49  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLE--------LFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaa 153
Cdd:cd05103  152 FVEEKSLSDVEeeeagqedLYKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLAR---- 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 pgEVYT--DYV-------ATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDQLYhimmCLgnlip 223
Cdd:cd05103  228 --DIYKdpDYVrkgdarlPLKWM-APETIFDRV-YTIQSDVWSFGVLLWEIFsLGASPYPG-VKIDEEF----CR----- 293
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 224 RHQElfnknpvfaGVRLpeikeREPlERRYPKLSEVVIDlakkCLHIDPDKRPFCAELLHH 284
Cdd:cd05103  294 RLKE---------GTRM-----RAP-DYTTPEMYQTMLD----CWHGEPSQRPTFSELVEH 335
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
10-233 5.15e-17

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 82.06  E-value: 5.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYG---MVMKCRNKDTGRIVA---IKKFLESDDDKMVKKIamrEIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFv 83
Cdd:cd05582    3 LGQGSFGkvfLVRKITGPDAGTLYAmkvLKKATLKVRDRVRTKM---ERDILADVNHPFIVKLHYAFQTEGKLYLILDF- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 dhtiLDDLELFpNGLDYQV------VQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-TLAAPGE 156
Cdd:cd05582   79 ----LRGGDLF-TRLSKEVmfteedVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEKK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 VYTdYVATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMC-LG---NLIPRHQ----EL 228
Cdd:cd05582  154 AYS-FCGTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAkLGmpqFLSPEAQsllrAL 231

                 ....*
gi 578809600 229 FNKNP 233
Cdd:cd05582  232 FKRNP 236
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
9-212 6.71e-17

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 80.36  E-value: 6.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDK--MVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14189    8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKphQREKI-VNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRW 166
Cdd:cd14189   87 SLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGTPN 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 167 YRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPgDSDIDQLY 212
Cdd:cd14189  167 YLAPEVLLRQ-GHGPESDVWSLGCVMYTLLCGNPPFE-TLDLKETY 210
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
5-281 8.92e-17

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 80.54  E-value: 8.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLVGEGSYGMVMK---CRNKDTGRI-VAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKkRWYLVF 80
Cdd:cd05057   10 EKGKVLGSGAFGTVYKgvwIPEGEKVKIpVAIKVLREETGPKANEEI-LDEAYVMASVDHPHLVRLLGICLSS-QVQLIT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYT 159
Cdd:cd05057   88 QLMPLGCLLDYVRNHRDnIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYH 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 ---DYVATRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMFMgeplfpgdsdidqlyhimmclgnliprhqelFNKNPvFA 236
Cdd:cd05057  168 aegGKVPIKWM-ALESIQ-YRIYTHKSDVWSYGVTVWELMT-------------------------------FGAKP-YE 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 237 GVRLPEIKERepLER--RYPKLSEVVID---LAKKCLHIDPDKRPFCAEL 281
Cdd:cd05057  214 GIPAVEIPDL--LEKgeRLPQPPICTIDvymVLVKCWMIDAESRPTFKEL 261
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
9-282 1.11e-16

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 79.74  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKFLESDDDKMVKKIA--MREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14061    1 VIGVGGFGKVYRGIWR--GEEVAVKAARQDPDEDISVTLEnvRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHN---IIHRDIKPENILVS--------QSGVVKLCDFGFARtlaapg 155
Cdd:cd14061   79 ALNRV-LAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILeaienedlENKTLKITDFGLAR------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVY----TDYVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGdsdIDQL---YHIMMclgnliprhqel 228
Cdd:cd14061  152 EWHkttrMSAAGTYAWMAPEVIKSST-FSKASDVWSYGVLLWELLTGEVPYKG---IDGLavaYGVAV------------ 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 229 fNKnpvfagVRLPeIKEREPlerrypklsEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd14061  216 -NK------LTLP-IPSTCP---------EPFAQLMKDCWQPDPHDRPSFADIL 252
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
13-197 1.14e-16

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 80.45  E-value: 1.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  13 GSYGMVMKCRNKDtgRIVAIKKFLESDDDKMVkkiAMREIKLLKQLRHENLVNLLEVCK----KKKRWYLVFEFVDHTIL 88
Cdd:cd14053    6 GRFGAVWKAQYLN--RLVAVKIFPLQEKQSWL---TEREIYSLPGMKHENILQFIGAEKhgesLEAEYWLITEFHERGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLeLFPNGLDYQVVQKYLFQIINGIGFCHS----------HNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA---PG 155
Cdd:cd14053   81 CDY-LKGNVISWNELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPgksCG 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 578809600 156 EVYtDYVATRWYRAPELLVGDVKYGK----AVDVWAIGCLVTEMFM 197
Cdd:cd14053  160 DTH-GQVGTRRYMAPEVLEGAINFTRdaflRIDMYAMGLVLWELLS 204
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1-211 1.20e-16

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 83.63  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600    1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLE--VCKKKKRWYL 78
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDrfLNKANQKLYI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   79 VFEFVD-----HTILDDLELFPNGLDYQVVQkYLFQIINGIGFCHS-------HNIIHRDIKPENILVSQS--------- 137
Cdd:PTZ00266   92 LMEFCDagdlsRNIQKCYKMFGKIEEHAIVD-ITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGirhigkita 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  138 --------GVVKLCDFGFARTLAAPGEVYTdYVATRWYRAPELLVGDVK-YGKAVDVWAIGCLVTEMFMGEPLFPGDSDI 208
Cdd:PTZ00266  171 qannlngrPIAKIGDFGLSKNIGIESMAHS-CVGTPYYWSPELLLHETKsYDDKSDMWALGCIIYELCSGKTPFHKANNF 249

                  ...
gi 578809600  209 DQL 211
Cdd:PTZ00266  250 SQL 252
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
3-149 1.58e-16

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 79.42  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKkfLESDDDKMvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRW-YLVFE 81
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK--IEKKDSKH--PQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYnVMVMD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTiLDDLelfpngLDYQvvqKYLF----------QIINGIGFCHSHNIIHRDIKPENILV---SQSGVVKLCDFGFA 148
Cdd:cd14016   77 LLGPS-LEDL------FNKC---GRKFslktvlmladQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLA 146

                 .
gi 578809600 149 R 149
Cdd:cd14016  147 K 147
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
10-197 1.70e-16

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 80.36  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR--------------NKDTGR--IVAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKK 73
Cdd:cd05096   13 LGEGQFGEVHLCEvvnpqdlptlqfpfNVRKGRplLVAVK-ILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVDE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFE---------FVDHTILDDLELFPNGLD----------YQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV 134
Cdd:cd05096   92 DPLCMITEymengdlnqFLSSHHLDDKEENGNDAVppahclpaisYSSLLHVALQIASGMKYLSSLNFVHRDLATRNCLV 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 135 SQSGVVKLCDFGFARTLAApGEVY----TDYVATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMFM 197
Cdd:cd05096  172 GENLTIKIADFGMSRNLYA-GDYYriqgRAVLPIRWMAWECILMG--KFTTASDVWAFGVTLWEILM 235
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
4-288 2.08e-16

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 80.35  E-value: 2.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYG---MVMKCRNKDTGRIVAIKkflesdddkMVKKIAM-REIKLLKQLRHENlvNLLEVCKKKKrwYLV 79
Cdd:cd05614    2 FELLKVLGTGAYGkvfLVRKVSGHDANKLYAMK---------VLRKAALvQKAKTVEHTRTER--NVLEHVRQSP--FLV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 ---FEFVD----HTILDDL---ELFPNglDYQ-------VVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKL 142
Cdd:cd05614   69 tlhYAFQTdaklHLILDYVsggELFTH--LYQrdhfsedEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 143 CDFGFARTLAAPGEVYT-DYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHImmclgnl 221
Cdd:cd05614  147 TDFGLSKEFLTEEKERTySFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEV------- 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 222 iprHQELFNKNPVFAgvrlpeikereplerryPKLSEVVIDLAKKCLHIDPDKR----PFCA-ELLHHDFFQ 288
Cdd:cd05614  220 ---SRRILKCDPPFP-----------------SFIGPVARDLLQKLLCKDPKKRlgagPQGAqEIKEHPFFK 271
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
27-287 2.19e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 80.69  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  27 GRIVAIKKflESDDDKMVKKIAMR-----EIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFPNGLDYQ 101
Cdd:PHA03209  80 GRVFVATK--PGQPDPVVLKIGQKgttliEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPID 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 102 ---VVQKylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-TLAAP------GEVYTDyvatrwyrAPE 171
Cdd:PHA03209 158 qalIIEK---QILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQfPVVAPaflglaGTVETN--------APE 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 172 LLVGDvKYGKAVDVWAIGCLVTEM-------FMGEPLFPGDSDIDQLYHIMMCLGNLiPRHQELFNKNPvfaGVRL-PEI 243
Cdd:PHA03209 227 VLARD-KYNSKADIWSAGIVLFEMlaypstiFEDPPSTPEEYVKSCHSHLLKIISTL-KVHPEEFPRDP---GSRLvRGF 301
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 244 KEREPLER----RYPKLSEVVID-----LAKKCLHIDPDKRPFCAELLHHDFF 287
Cdd:PHA03209 302 IEYASLERqpytRYPCFQRVNLPidgefLVHKMLTFDAAMRPSAEEILNYPMF 354
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
10-283 2.34e-16

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 79.14  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRiVAIKKFLESdddKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TIL 88
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQYK-VAIKAIREG---AMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENgCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRW-- 166
Cdd:cd05114   88 NYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVL--DDQYTSSSGAKFpv 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 -YRAPELLVGDvKYGKAVDVWAIGCLVTEMFM-GEPLFPGDSDIDQLYHIMmclgnliprhqelfnknpvfAGVRLPEik 244
Cdd:cd05114  166 kWSPPEVFNYS-KFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVS--------------------RGHRLYR-- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 578809600 245 ereplerryPKL-SEVVIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd05114  223 ---------PKLaSKSVYEVMYSCWHEKPEGRPTFADLLR 253
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
2-215 2.39e-16

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 80.85  E-value: 2.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKKIAMREIKLLKQLRHEN----LVNLLEVCKKKKRWY 77
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKAD---MLEKEQVGHIRAERDILVEAdslwVVKMFYSFQDKLNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL--AAPG 155
Cdd:cd05628   78 LIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLkkAHRT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVY--------TDY-------------------------VATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05628  158 EFYrnlnhslpSDFtfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFM-QTGYNKLCDWWSLGVIMYEMLIGYPPF 236
                        250
                 ....*....|...
gi 578809600 203 PGDSDIDQLYHIM 215
Cdd:cd05628  237 CSETPQETYKKVM 249
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
10-215 2.60e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 79.67  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----NKDT-GRIVAIK-KFLESDDDKMVKKIAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd05098   21 LGEGCFGQVVLAEaiglDKDKpNRVTKVAvKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDL--ELFPNGLDY-----QVVQKYL---------FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd05098  101 ASKGNLREYlqARRPPGMEYcynpsHNPEEQLsskdlvscaYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFG 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 147 FARTLAapgevYTDY--------VATRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDQLYHIM 215
Cdd:cd05098  181 LARDIH-----HIDYykkttngrLPVKWM-APEALF-DRIYTHQSDVWSFGVLLWEIFtLGGSPYPG-VPVEELFKLL 250
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
9-281 2.74e-16

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 78.84  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKFLESDDDKMVKKiamrEIKLLKQLRHENLVNLLEVCKKKKrwYLVFEFVDHTIL 88
Cdd:cd14068    1 LLGDGGFGSVYRAVYR--GEDVAVKIFNKHTSFRLLRQ----ELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV-----SQSGVVKLCDFGFARTLAAPGEVYTDyv 162
Cdd:cd14068   73 DALLQQDNAsLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIKTSE-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLVGDVKYGKAVDVWAIGCLvtemfmgeplfpgdsdidqLYHIMMCLGNLIprhqelfnknpvfAGVRLPE 242
Cdd:cd14068  151 GTPGFRAPEVARGNVIYNQQADVYSFGLL-------------------LYDILTCGERIV-------------EGLKFPN 198
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 243 IKEREPLERRYPKLSE--------VVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd14068  199 EFDELAIQGKLPDPVKeygcapwpGVEALIKDCLKENPQCRPTSAQV 245
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
10-276 3.08e-16

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 78.42  E-value: 3.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMV-MKCRNKDTGriVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDHTIL 88
Cdd:cd14203    3 LGQGCFGEVwMGTWNGTTK--VAIKTL---KPGTMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKGSL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtLAAPGEvYTDYVATRW 166
Cdd:cd14203   77 LDFLKDGEGKYLKLPQlvDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLAR-LIEDNE-YTARQGAKF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 167 ---YRAPELLVgdvkYGKAV---DVWAIGCLVTEMFM-GEPLFPGDSDIDQLyhimmclgnliprhqelfnkNPVFAGVR 239
Cdd:cd14203  155 pikWTAPEAAL----YGRFTiksDVWSFGILLTELVTkGRVPYPGMNNREVL--------------------EQVERGYR 210
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 578809600 240 LPeikerEPlerryPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd14203  211 MP-----CP-----PGCPESLHELMCQCWRKDPEERP 237
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
1-207 3.21e-16

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 78.74  E-value: 3.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVgEGSYGMVMKCRNKDTGR-----IVAIKKFleSDDDKMVKKIaMREikllkqlrHENLVNLLEVCKKKKR 75
Cdd:PHA03390  16 CEIVKKLKLI-DGKFGKVSVLKHKPTQKlfvqkIIKAKNF--NAIEPMVHQL-MKD--------NPNFIKLYYSVTTLKG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV-VKLCDFGFARTLAAP 154
Cdd:PHA03390  84 HVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYGLCKIIGTP 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 578809600 155 GEvytdYVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSD 207
Cdd:PHA03390 164 SC----YDGTLDYFSPEKIKGHN-YDVSFDWWAVGVLTYELLTGKHPFKEDED 211
pknD PRK13184
serine/threonine-protein kinase PknD;
1-275 3.53e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.74  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLES-DDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:PRK13184   1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDL-------ELFPNGLDYQVVQKYLFQIIN----GIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:PRK13184  81 MPYIEGYTLKSLlksvwqkESLSKELAEKTSVGAFLSIFHkicaTIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 149 RTLAAPGEVYTDY------------------VATRWYRAPELLVGdVKYGKAVDVWAIGCLvtemfmgeplfpgdsdidq 210
Cdd:PRK13184 161 IFKKLEEEDLLDIdvdernicyssmtipgkiVGTPDYMAPERLLG-VPASESTDIYALGVI------------------- 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 211 LYHiMMCLGNliPRHQELFNKNPVFAGVRLPEikEREPLERRYPKLSEVVIdlakKCLHIDPDKR 275
Cdd:PRK13184 221 LYQ-MLTLSF--PYRRKKGRKISYRDVILSPI--EVAPYREIPPFLSQIAM----KALAVDPAER 276
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
9-282 5.27e-16

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 78.16  E-value: 5.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGR-----IVAIKKFLESDDDKMVKKiamrEIKLLKQL-RHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd05047    2 VIGEGNFGQVLKARIKKDGLrmdaaIKRMKEYASKDDHRDFAG----ELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDD-------LELFP---------NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd05047   78 APHGNLLDflrksrvLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTlaapGEVYTD----YVATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEM--FMGEPlfpgdsdidqlYHIMMClgn 220
Cdd:cd05047  158 LSRG----QEVYVKktmgRLPVRWM-AIESLNYSV-YTTNSDVWSYGVLLWEIvsLGGTP-----------YCGMTC--- 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 221 liprhQELFNKNPvfAGVRLpeikeREPLerrypKLSEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd05047  218 -----AELYEKLP--QGYRL-----EKPL-----NCDDEVYDLMRQCWREKPYERPSFAQIL 262
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
10-196 5.41e-16

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 77.99  E-value: 5.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKcrNKDTGRIVAIKKfLESDddkMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDHTILD 89
Cdd:cd05083   14 IGEGEFGAVLQ--GEYMGQKVAVKN-IKCD---VTAQAFLEETAVMTKLQHKNLVRLLGVILHNG-LYIVMELMSKGNLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLeLFPNGLD----YQVVQkYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlAAPGEVYTDYVATR 165
Cdd:cd05083   87 NF-LRSRGRAlvpvIQLLQ-FSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK--VGSMGVDNSRLPVK 162
                        170       180       190
                 ....*....|....*....|....*....|.
gi 578809600 166 WyRAPELLvGDVKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05083  163 W-TAPEAL-KNKKFSSKSDVWSYGVLLWEVF 191
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
10-196 5.61e-16

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 78.50  E-value: 5.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----------------NKDTGRIVAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKK 73
Cdd:cd05095   13 LGEGQFGEVHLCEaegmekfmdkdfalevSENQPVLVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  74 KRWYLVFEFVDHTILDD----------LELFPNGL--DYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVK 141
Cdd:cd05095   92 DPLCMITEYMENGDLNQflsrqqpegqLALPSNALtvSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 142 LCDFGFARTLAApGEVY----TDYVATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05095  172 IADFGMSRNLYS-GDYYriqgRAVLPIRWMSWESILLG--KFTTASDVWAFGVTLWETL 227
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
3-284 5.71e-16

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 79.68  E-value: 5.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESdddKMVKKIAMREIKLLKQLR--------HENLVNLLE------ 68
Cdd:cd14218   11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSA---VHYTETAVDEIKLLKCVRdsdpsdpkRETIVQLIDdfkisg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 -----VCkkkkrwyLVFEFVDHTILD-DLELFPNGLDYQVVQKYLFQIINGIGFCHSH-NIIHRDIKPENIL--VSQSGV 139
Cdd:cd14218   88 vngvhVC-------MVLEVLGHQLLKwIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILmcVDEGYV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 140 VKLC-------------------DFGFARTLAAPGEV----------------------YTDYVATRWYRAPELLVGdVK 178
Cdd:cd14218  161 RRLAaeatiwqqagapppsgssvSFGASDFLVNPLEPqnadkirvkiadlgnacwvhkhFTEDIQTRQYRALEVLIG-AE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 179 YGKAVDVWAIGCLVTEMFMGEPLFPGDS------DIDQLYHIMMCLGNlIPRH--------QELFNKNPVFAGVR----- 239
Cdd:cd14218  240 YGTPADIWSTACMAFELATGDYLFEPHSgedytrDEDHIAHIVELLGD-IPPHfalsgrysREYFNRRGELRHIKnlkhw 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 240 -LPEI---KEREPLERRyPKLSEVVIDLakkcLHIDPDKRPFCAELLHH 284
Cdd:cd14218  319 gLYEVlveKYEWPLEQA-AQFTDFLLPM----MEFLPEKRATAAQCLQH 362
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
9-197 7.08e-16

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 78.25  E-value: 7.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKFLESDDDKMVKKiamREIKLLKQLRHENLVNLLEVCKKK----KRWYLVFEFVD 84
Cdd:cd13998    2 VIGKGRFGEVWKASLK--NEPVAVKIFSSRDKQSWFRE---KEIYRTPMLKHENILQFIAADERDtalrTELWLVTAFHP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSH---------NIIHRDIKPENILVSQSGVVKLCDFGFARTLaAPG 155
Cdd:cd13998   77 NGSL*DY-LSLHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLAVRL-SPS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 156 EVYTD-----YVATRWYRAPELLVGDVKYG-----KAVDVWAIGCLVTEMFM 197
Cdd:cd13998  155 TGEEDnanngQVGTKRYMAPEVLEGAINLRdfesfKRVDIYAMGLVLWEMAS 206
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
10-215 7.51e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 78.52  E-value: 7.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----NKDTGR---IVAIKKFlesDDDKMVKKIA--MREIKLLKQL-RHENLVNLLEVCKKKKRWYLV 79
Cdd:cd05101   32 LGEGCFGQVVMAEavgiDKDKPKeavTVAVKML---KDDATEKDLSdlVSEMEMMKMIgKHKNIINLLGACTQDGPLYVI 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVDHTILDDL--ELFPNGLDY----------QVVQKYL----FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLC 143
Cdd:cd05101  109 VEYASKGNLREYlrARRPPGMEYsydinrvpeeQMTFKDLvsctYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIA 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 144 DFGFARTLAApgevyTDY--------VATRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDQLYHI 214
Cdd:cd05101  189 DFGLARDINN-----IDYykkttngrLPVKWM-APEALF-DRVYTHQSDVWSFGVLMWEIFtLGGSPYPG-IPVEELFKL 260

                 .
gi 578809600 215 M 215
Cdd:cd05101  261 L 261
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
4-206 1.16e-15

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 78.13  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLGLVGEGSYGMVMKCRNKDTGRIVAIKkFLESDDDKMVKKIAM----REIklLKQLRHENLVNLLEVCKKKKRWYLV 79
Cdd:cd05598    3 FEKIKTIGVGAFGEVSLVRKKDTNALYAMK-TLRKKDVLKRNQVAHvkaeRDI--LAEADNEWVVKLYYSFQDKENLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  80 FEFVD----HTILDDLELFPNGLdyqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGF-------- 147
Cdd:cd05598   80 MDYIPggdlMSLLIKKGIFEEDL----ARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwth 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 148 ------ARTLaapgevytdyVATRWYRAPELLVgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd05598  156 dskyylAHSL----------VGTPNYIAPEVLL-RTGYTQLCDWWSVGVILYEMLVGQPPFLAQT 209
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
3-281 1.16e-15

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 77.98  E-value: 1.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKfLESDDDKMVKkIAMREIKLLK--QLRHENLVN--------------- 65
Cdd:cd13977    1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKK-IRCNAPENVE-LALREFWALSsiQRQHPNVIQleecvlqrdglaqrm 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  66 ------------LLEVCKKKKR----------WYlVFEFVDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNII 123
Cdd:cd13977   79 shgssksdlyllLVETSLKGERcfdprsacylWF-VMEFCDGGDMNEY-LLSRRPDRQTNTSFMLQLSSALAFLHRNQIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 124 HRDIKPENILVSQ---SGVVKLCDFGFARTLAAPGEVYTDYV-----------ATRWYRAPELLVGdvKYGKAVDVWAIG 189
Cdd:cd13977  157 HRDLKPDNILISHkrgEPILKVADFGLSKVCSGSGLNPEEPAnvnkhflssacGSDFYMAPEVWEG--HYTAKADIFALG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 190 CLVTEMFmgEPLFPGDSDIDQlyhimMCLGNLIPRHQELFnknPVF-AGVRLPEIKEREPLERRyPKLSEVVIDLAKKCL 268
Cdd:cd13977  235 IIIWAMV--ERITFRDGETKK-----ELLGTYIQQGKEIV---PLGeALLENPKLELQIPLKKK-KSMNDDMKQLLRDML 303
                        330
                 ....*....|...
gi 578809600 269 HIDPDKRPFCAEL 281
Cdd:cd13977  304 AANPQERPDAFQL 316
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
11-281 1.27e-15

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 77.00  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCR-NKDTGRI--VAIKKFlesDDDKMVKKIAM----REIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFV 83
Cdd:cd05040    4 GDGSFGVVRRGEwTTPSGKViqVAVKCL---KSDVLSQPNAMddflKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 D-HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEVYTDYV 162
Cdd:cd05040   80 PlGSLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRAL----PQNEDHY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYR-------APELLvgdvKYGK---AVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYHIMmclgnliprhqelfnk 231
Cdd:cd05040  156 VMQEHRkvpfawcAPESL----KTRKfshASDVWMFGVTLWEMFtYGEEPWLGLNGSQILEKID---------------- 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 232 npvfagvrlpeiKEREPLERryPK-LSEVVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd05040  216 ------------KEGERLER--PDdCPQDIYNVMLQCWAHKPADRPTFVAL 252
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
9-216 1.34e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 77.00  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMkcRNKDTGRIVAIKKFLESDDDKMVKKI--AMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14145   13 IIGIGGFGKVY--RAIWIGDEVAVKAARHDPDEDISQTIenVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHNI---IHRDIKPENILVSQ--------SGVVKLCDFGFAR------ 149
Cdd:cd14145   91 PLNRV-LSGKRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEkvengdlsNKILKITDFGLARewhrtt 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 150 TLAAPGevytdyvaTRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMM 216
Cdd:cd14145  170 KMSAAG--------TYAWMAPEVIRSSM-FSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAM 227
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
10-225 1.38e-15

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 76.80  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMK--CRNKdtgrIVAIKKF------LESDDDKMVkkiamREIKLLKQLRHENLVNLLEVC-KKKKRWYLVF 80
Cdd:cd14064    1 IGSGSFGKVYKgrCRNK----IVAIKRYrantycSKSDVDMFC-----REVSILCRLNHPCVIQFVGAClDDPSQFAIVT 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHTILDDLElfpNG----LDYQVVQKYLFQIINGIGFCH--SHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA- 153
Cdd:cd14064   72 QYVSGGSLFSLL---HEqkrvIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSl 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 --------PGEVytdyvatRWYrAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF----PGDSDIDQLY-HIMMCLGN 220
Cdd:cd14064  149 dednmtkqPGNL-------RWM-APEVFTQCTRYSIKADVFSYALCLWELLTGEIPFahlkPAAAAADMAYhHIRPPIGY 220

                 ....*
gi 578809600 221 LIPRH 225
Cdd:cd14064  221 SIPKP 225
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
10-206 1.57e-15

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 76.54  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKkFLESdddKMVKK-IAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVK-FVSK---KMKKKeQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVS---QSGVVKLCDFGFARTLAAPGEVYTdYVATR 165
Cdd:cd14115   77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGHRHVHH-LLGNP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 578809600 166 WYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPGDS 206
Cdd:cd14115  156 EFAAPEVIQG-TPVSLATDIWSIGVLTYVMLSGVSPFLDES 195
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
10-207 1.72e-15

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 76.60  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMV-MKCRNKDTGriVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDHTIL 88
Cdd:cd05073   19 LGAGQFGEVwMATYNKHTK--VAVKTM---KPGSMSVEAFLAEANVMKTLQHDKLVKLHAVVTKEP-IYIITEFMAKGSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLF--QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgevyTDYVA--- 163
Cdd:cd05073   93 LDFLKSDEGSKQPLPKLIDFsaQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIED-----NEYTAreg 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 164 ----TRWyRAPELlvgdVKYGKAV---DVWAIGCLVTEMF-MGEPLFPGDSD 207
Cdd:cd05073  168 akfpIKW-TAPEA----INFGSFTiksDVWSFGILLMEIVtYGRIPYPGMSN 214
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
110-288 1.85e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 78.11  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 110 IINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArtlAAPGEV----YTDYVATRWYRAPELLVGDvKYGKAVDV 185
Cdd:PHA03212 191 VLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAA---CFPVDInankYYGWAGTIATNAPELLARD-PYGPAVDI 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 186 WAIGCLVTEMFMGE-PLFPG---DSDIDQLYHIMMclgnLIPRHQELFNKNPVFAGVRLPEI-------KEREPLER-RY 253
Cdd:PHA03212 267 WSAGIVLFEMATCHdSLFEKdglDGDCDSDRQIKL----IIRRSGTHPNEFPIDAQANLDEIyiglakkSSRKPGSRpLW 342
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809600 254 PKLSEVVIDLAK---KCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:PHA03212 343 TNLYELPIDLEYlicKMLAFDAHHRPSAEALLDFAAFQ 380
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
10-199 1.93e-15

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 76.26  E-value: 1.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGR---IVAIKKFLESDDDKMvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd05033   12 IGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSGYSDKQ-RLDFLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLeLFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY--- 161
Cdd:cd05033   91 SLDKF-LRENDGKFTVTQlvGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEATYTTKggk 169
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 578809600 162 VATRWyRAPElLVGDVKYGKAVDVWAIGCLVTE-MFMGE 199
Cdd:cd05033  170 IPIRW-TAPE-AIAYRKFTSASDVWSFGIVMWEvMSYGE 206
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
3-284 2.15e-15

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 77.76  E-value: 2.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDdkmVKKIAMREIKLLKQLRH--------ENLVNLLEVCK--- 71
Cdd:cd14216   11 RYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEH---YTETALDEIKLLKSVRNsdpndpnrEMVVQLLDDFKisg 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  72 -KKKRWYLVFEFVDHTILD-DLELFPNGLDYQVVQKYLFQIINGIGFCHSH-NIIHRDIKPENILVSQSGV--------- 139
Cdd:cd14216   88 vNGTHICMVFEVLGHHLLKwIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSVNEQyirrlaaea 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 140 ---------------------VKLCDFGFARTLAapgEVYTDYVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMG 198
Cdd:cd14216  168 tewqrnflvnplepknaeklkVKIADLGNACWVH---KHFTEDIQTRQYRSLEVLIGS-GYNTPADIWSTACMAFELATG 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 199 EPLFPGDS------DIDQLYHIMMCLGnLIPRH--------QELFNKNPvfagvRLPEIKEREP------LERRYPKLSE 258
Cdd:cd14216  244 DYLFEPHSgedysrDEDHIALIIELLG-KVPRKlivagkysKEFFTKKG-----DLKHITKLKPwglfevLVEKYEWSQE 317
                        330       340
                 ....*....|....*....|....*....
gi 578809600 259 ---VVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14216  318 eaaGFTDFLLPMLELIPEKRATAAECLRH 346
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
8-198 2.30e-15

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 76.40  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   8 GLVGEGSYGMVMKCRNKDTGRIVAIKKFlesdddkMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFefvdhti 87
Cdd:cd13991   12 LRIGRGSFGEVHRMEDKQTGFQCAVKKV-------RLEVFRAEELMACAGLTSPRVVPLYGAVREGP-WVNIF------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 lddLELFPNGLDYQVVQK-----------YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV-VKLCDFGFARTLAAPG 155
Cdd:cd13991   77 ---MDLKEGGSLGQLIKEqgclpedralhYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAECLDPDG 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 156 ---EVYT-DYV-ATRWYRAPELLVGDVKYGKaVDVWAIGCLVTEMFMG 198
Cdd:cd13991  154 lgkSLFTgDYIpGTETHMAPEVVLGKPCDAK-VDVWSSCCMMLHMLNG 200
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
10-283 2.46e-15

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 76.38  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRnKDTGRIVAIKKFLESDDDKMVKKIAmREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILD 89
Cdd:cd14664    1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHGFQ-AEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DL--ELFPNG--LDYQVVQKYLFQIINGIGFCHSH---NIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPG-EVYTDY 161
Cdd:cd14664   79 ELlhSRPESQppLDWETRQRIALGSARGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDsHVMSSV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 162 VATRWYRAPElLVGDVKYGKAVDVWAIGCLVTEMFMGE---PLFPGDSDIDqlyhIMMCLGNLIPRHQELFNKNPVFAGv 238
Cdd:cd14664  159 AGSYGYIAPE-YAYTGKVSEKSDVYSYGVVLLELITGKrpfDEAFLDDGVD----IVDWVRGLLEEKKVEALVDPDLQG- 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 239 rlpeikereplerrYPKLSEV--VIDLAKKCLHIDPDKRPFCAELLH 283
Cdd:cd14664  233 --------------VYKLEEVeqVFQVALLCTQSSPMERPTMREVVR 265
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
10-215 3.63e-15

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 76.60  E-value: 3.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----NKDTGR---IVAIKKFLESDDDKMVKKIaMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd05100   20 LGEGCFGQVVMAEaigiDKDKPNkpvTVAVKMLKDDATDKDLSDL-VSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDL--ELFPNGLDY----------QVVQKYL----FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd05100   99 YASKGNLREYlrARRPPGMDYsfdtcklpeeQLTFKDLvscaYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADF 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 146 GFAR---TLAAPGEVYTDYVATRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDQLYHIM 215
Cdd:cd05100  179 GLARdvhNIDYYKKTTNGRLPVKWM-APEALF-DRVYTHQSDVWSFGVLLWEIFtLGGSPYPG-IPVEELFKLL 249
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
10-196 4.00e-15

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 75.77  E-value: 4.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVM--KCRN---KDTGRIVAIKKFLESDDDkmVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05092   13 LGEGAFGKVFlaECHNllpEQDKMLVAVKALKEATES--ARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILD--------DLELFPNGLDYQVVQKYL-------FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR 149
Cdd:cd05092   91 HGDLNrflrshgpDAKILDGGEGQAPGQLTLgqmlqiaSQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSR 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 150 tlaapgEVY-TDY--------VATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05092  171 ------DIYsTDYyrvggrtmLPIRWMPPESILYR--KFTTESDIWSFGVVLWEIF 218
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
9-211 4.30e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 75.46  E-value: 4.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKfLESDDDKMVKKIA---MREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd14146    1 IIGVGGFGKVYRATWK--GQEVAVKA-ARQDPDEDIKATAesvRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLELFPNG---------LDYQVVQKYLFQIINGIGFCHSHN---IIHRDIKPENILVSQ--------SGVVKLCDF 145
Cdd:cd14146   78 GTLNRALAAANAapgprrarrIPPHILVNWAVQIARGMLYLHEEAvvpILHRDLKSSNILLLEkiehddicNKTLKITDF 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 146 GFARTLAAPGEVYTdyVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPGdsdIDQL 211
Cdd:cd14146  158 GLAREWHRTTKMSA--AGTYAWMAPEVIKSSL-FSKGSDIWSYGVLLWELLTGEVPYRG---IDGL 217
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
9-207 5.11e-15

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 75.19  E-value: 5.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNK-----DTGRIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFV 83
Cdd:cd05046   12 TLGRGEFGEVFLAKAKgieeeGGETLVLVKA-LQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 DhtiLDDLELF------------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTl 151
Cdd:cd05046   91 D---LGDLKQFlratkskdeklkPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKD- 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 152 aapgeVYTD--------YVATRWYrAPELLVGDvKYGKAVDVWAIGCLVTEMF-MGEPLFPGDSD 207
Cdd:cd05046  167 -----VYNSeyyklrnaLIPLRWL-APEAVQED-DFSTKSDVWSFGVLMWEVFtQGELPFYGLSD 224
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
18-212 5.93e-15

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 75.37  E-value: 5.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  18 VMKCRNKDtgRIVAIKKFLESDDDKMVKKIAmREIKLLKQ--LRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFP 95
Cdd:cd13980   16 VARARHDE--GLVVVKVFVKPDPALPLRSYK-QRLEEIRDrlLELPNVLPFQKVIETDKAAYLIRQYVKYNLYDRISTRP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  96 NgldYQVVQK--YLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF-GFART-LAA--PGEvYTDYVAT----R 165
Cdd:cd13980   93 F---LNLIEKkwIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFaSFKPTyLPEdnPAD-FSYFFDTsrrrT 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 166 WYRAPE------LLVGDVKYG-----KAVDVWAIGCLVTEMFM-GEPLFpgdsDIDQLY 212
Cdd:cd13980  169 CYIAPErfvdalTLDAESERRdgeltPAMDIFSLGCVIAELFTeGRPLF----DLSQLL 223
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
1-205 6.31e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 77.43  E-value: 6.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKC------RNKDTGRIVAIKKFLESDDDKMVKKIAM----------REIKLLKQLRHENLV 64
Cdd:PHA03210 147 LAHFRVIDDLPAGAFGKIFICalrastEEAEARRGVNSTNQGKPKCERLIAKRVKagsraaiqleNEILALGRLNHENIL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  65 NLLEVCKKKKRWYLV-----FEFVDHTILDDLELFPNGLDYQVvQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGV 139
Cdd:PHA03210 227 KIEEILRSEANTYMItqkydFDLYSFMYDEAFDWKDRPLLKQT-RAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGK 305
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 140 VKLCDFGFARTLAAPGEVYtDY--VATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGD 205
Cdd:PHA03210 306 IVLGDFGTAMPFEKEREAF-DYgwVGTVATNSPEILAGD-GYCEITDIWSCGLILLDMLSHDFCPIGD 371
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
2-202 7.30e-15

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 76.43  E-value: 7.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDddkMVKKIAMREIKLLKQLRHEN----LVNLLEVCKKKKRWY 77
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSE---MFKKDQLAHVKAERDVLAESdspwVVSLYYSFQDAQYLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  78 LVFEFVD----HTILDDLELFPNgldyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR---- 149
Cdd:cd05629   78 LIMEFLPggdlMTMLIKYDTFSE----DVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTgfhk 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 ---------------------------------TLAAPGEVYT----------DYVATRWYRAPELLVGDvKYGKAVDVW 186
Cdd:cd05629  154 qhdsayyqkllqgksnknridnrnsvavdsinlTMSSKDQIATwkknrrlmaySTVGTPDYIAPEIFLQQ-GYGQECDWW 232
                        250
                 ....*....|....*.
gi 578809600 187 AIGCLVTEMFMGEPLF 202
Cdd:cd05629  233 SLGAIMFECLIGWPPF 248
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
13-276 8.73e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 74.46  E-value: 8.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  13 GSYGMVMKCRNKDTGRIVaIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH-TILDDL 91
Cdd:cd14027    4 GGFGKVSLCFHRTQGLVV-LKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKgNLMHVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  92 ELFPNGLdyQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA-------------RTLAAPGEVY 158
Cdd:cd14027   83 KKVSVPL--SVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehNEQREVDGTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVATRWYRAPELLVG-DVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHiMMCLGNliprhqelfnkNPvfag 237
Cdd:cd14027  161 KKNAGTLYYMAPEHLNDvNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIM-CIKSGN-----------RP---- 224
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 578809600 238 vRLPEIKEREPLErrypklsevVIDLAKKCLHIDPDKRP 276
Cdd:cd14027  225 -DVDDITEYCPRE---------IIDLMKLCWEANPEARP 253
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
9-204 9.46e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 74.30  E-value: 9.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMkcRNKDTGRIVAIKKFLES-DDDKMVKKIAMR-EIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14147   10 VIGIGGFGKVY--RGSWRGELVAVKAARQDpDEDISVTAESVRqEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDlELFPNGLDYQVVQKYLFQIINGIGFCHSHNI---IHRDIKPENILVSQSGV--------VKLCDFGFARTLAAPG 155
Cdd:cd14147   88 PLSR-ALAGRRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehktLKITDFGLAREWHKTT 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 156 EVYTdyVATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGEPLFPG 204
Cdd:cd14147  167 QMSA--AGTYAWMAPEVIKAST-FSKGSDVWSFGVLLWELLTGEVPYRG 212
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
88-204 1.18e-14

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 75.02  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPngLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaapgEVYT--DYV--- 162
Cdd:cd05102  161 VDDLWQSP--LTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLAR------DIYKdpDYVrkg 232
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 163 ----ATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPG 204
Cdd:cd05102  233 sarlPLKWM-APESIFDKV-YTTQSDVWSFGVLLWEIFsLGASPYPG 277
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
9-283 1.23e-14

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 73.99  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKD-----TGRI-VAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVfef 82
Cdd:cd05044    2 FLGSGAFGEVFEGTAKDilgdgSGETkVAVKTLRKGATDQEKAEF-LKEAHLMSNFKHPNILKLLGVCLDNDPQYII--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 vdhtilddLELFPNG--LDY------------QVVQKYLFQII----NGIGFCHSHNIIHRDIKPENILVSQSG----VV 140
Cdd:cd05044   78 --------LELMEGGdlLSYlraarptaftppLLTLKDLLSICvdvaKGCVYLEDMHFVHRDLAARNCLVSSKDyrerVV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 141 KLCDFGFARtlaapgEVY-TDY--------VATRWYrAPELLVgDVKYGKAVDVWAIGCLVTE-MFMGEPLFPGDSDIDQ 210
Cdd:cd05044  150 KIGDFGLAR------DIYkNDYyrkegeglLPVRWM-APESLV-DGVFTTQSDVWAFGVLMWEiLTLGQQPYPARNNLEV 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 211 LYHimmclgnliprhqelfnknpVFAGVRLpeikerepleRRYPKLSEVVIDLAKKCLHIDPDKRP---FCAELLH 283
Cdd:cd05044  222 LHF--------------------VRAGGRL----------DQPDNCPDDLYELMLRCWSTDPEERPsfaRILEQLQ 267
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
83-276 1.31e-14

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 75.83  E-value: 1.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLElfpNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD-- 160
Cdd:cd05105  222 VKNLLSDDGS---EGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKgs 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 -YVATRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDQLYHimmclgnliprhqelfnkNPVFAGV 238
Cdd:cd05105  299 tFLPVKWM-APESIF-DNLYTTLSDVWSYGILLWEIFsLGGTPYPG-MIVDSTFY------------------NKIKSGY 357
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809600 239 RLPEiKEREPLErrypklsevVIDLAKKCLHIDPDKRP 276
Cdd:cd05105  358 RMAK-PDHATQE---------VYDIMVKCWNSEPEKRP 385
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
10-238 1.34e-14

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 74.23  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKdtGRIVAIKKFLESDDDKMVKKiamREIKLLKQLRHENLVNLLEVCKKKK----RWYLVFEFVDH 85
Cdd:cd14056    3 IGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDSWFRE---TEIYQTVMLRHENILGFIAADIKSTgswtQLWLITEYHEH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLeLFPNGLDYQVVQKYLFQIINGIgfCHSHN----------IIHRDIKPENILVSQSGVVKLCDFGFA---RTLA 152
Cdd:cd14056   78 GSLYDY-LQRNTLDTEEALRLAYSAASGL--AHLHTeivgtqgkpaIAHRDLKSKNILVKRDGTCCIADLGLAvryDSDT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 APGEVYTDY-VATRWYRAPELL-----VGDVKYGKAVDVWAIGCLVTEM-------FMGEP-------LFPGDSDIDQLY 212
Cdd:cd14056  155 NTIDIPPNPrVGTKRYMAPEVLddsinPKSFESFKMADIYSFGLVLWEIarrceigGIAEEyqlpyfgMVPSDPSFEEMR 234
                        250       260
                 ....*....|....*....|....*.
gi 578809600 213 HImMCLGNLIPRHQELFNKNPVFAGV 238
Cdd:cd14056  235 KV-VCVEKLRPPIPNRWKSDPVLRSM 259
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
31-282 1.35e-14

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 74.36  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  31 AIKKFLESDDDKMVKKIAMR---EIKLLKQLRHENLVNLLEVCKKKK-RWYLVFEFVDHTILD--------DLELFPngl 98
Cdd:cd14001   32 AVKKINSKCDKGQRSLYQERlkeEAKILKSLNHPNIVGFRAFTKSEDgSLCLAMEYGGKSLNDlieeryeaGLGPFP--- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  99 dYQVVQKYLFQIINGIGFCHSH-NIIHRDIKPENILVSQS-GVVKLCDFGFARTLAAPGEVYTD----YVATRWYRAPEL 172
Cdd:cd14001  109 -AATILKVALSIARALEYLHNEkKILHGDIKSGNVLIKGDfESVKLCDFGVSLPLTENLEVDSDpkaqYVGTEPWKAKEA 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 173 LVGDVKYGKAVDVWAIGCLVTEMFM-----GEPLFPGDSDIDQLYhimmclgnliprhQELFNKNPVFAGVR--LPEIKE 245
Cdd:cd14001  188 LEEGGVITDKADIFAYGLVLWEMMTlsvphLNLLDIEDDDEDESF-------------DEDEEDEEAYYGTLgtRPALNL 254
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 578809600 246 rEPLERRYPKlsevVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd14001  255 -GELDDSYQK----VIELFYACTQEDPKDRPSAAHIV 286
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
10-281 1.40e-14

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 74.48  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTgrIVAIKKFLESD--DDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd14159    1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSelDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDlELFPNG----LDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVSQSGVVKLCDFG---FARTLAAPGE-- 156
Cdd:cd14159   79 LED-RLHCQVscpcLSWSQRLHVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGlarFSRRPKQPGMss 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 157 --VYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYhimmcLGNLIPRH---QELFNK 231
Cdd:cd14159  158 tlARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMEVDSCSPTKY-----LKDLVKEEeeaQHTPTT 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 232 NPVFAGVRLPEIKE---REPLERRY----PKLSEVVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd14159  233 MTHSAEAQAAQLATsicQKHLDPQAgpcpPELGIEISQLACRCLHRRAKKRPPMTEV 289
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
9-199 1.53e-14

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 73.85  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGR---IVAIKKFLESDDDKMvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05063   12 VIGAGEFGEVFRGILKMPGRkevAVAIKTLKPGYTEKQ-RQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLeLFPNGLDYQVVQkyLFQIINGIG----FCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA-PGEVYTD 160
Cdd:cd05063   91 GALDKY-LRDHDGEFSSYQ--LVGMLRGIAagmkYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDdPEGTYTT 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809600 161 Y---VATRWyRAPElLVGDVKYGKAVDVWAIGCLVTE-MFMGE 199
Cdd:cd05063  168 SggkIPIRW-TAPE-AIAYRKFTSASDVWSFGIVMWEvMSFGE 208
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
9-202 3.07e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 73.53  E-value: 3.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDdkmvkkiAMREIKL-LKQLRHENLVNLLEVC----KKKKRWYLVFEfv 83
Cdd:cd14170    9 VLGLGINGKVLQIFNKRTQEKFALKMLQDCPK-------ARREVELhWRASQCPHIVRIVDVYenlyAGRKCLLIVME-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  84 dhtILDDLELFP---NGLDYQVVQKYLFQIINGIG----FCHSHNIIHRDIKPENILVSQ---SGVVKLCDFGFAR---- 149
Cdd:cd14170   80 ---CLDGGELFSriqDRGDQAFTEREASEIMKSIGeaiqYLHSINIAHRDVKPENLLYTSkrpNAILKLTDFGFAKetts 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 578809600 150 --TLAAPgeVYTDYvatrwYRAPELLvGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14170  157 hnSLTTP--CYTPY-----YVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGYPPF 203
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
4-285 3.49e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 72.73  E-value: 3.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   4 YENLG--LVGEGSYGMV-----MKCRNKDTGRIVAIKKFLESDddkmvkkiamreIKLLKQLRHENLVNLLEVCKKKKRW 76
Cdd:cd13995    4 YRNIGsdFIPRGAFGKVylaqdTKTKKRMACKLIPVEQFKPSD------------VEIQACFRHENIAELYGALLWEETV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDH-TILDDLELFPNGLDYQV--VQKylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVkLCDFGFARTLAA 153
Cdd:cd13995   72 HLFMEAGEGgSVLEKLESCGPMREFEIiwVTK---HVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 154 PGEVYTDYVATRWYRAPELLVGDVKYGKAvDVWAIGCLVTEMFMGEP----LFPGDSDIDQLYHIMmclgnliprhqelf 229
Cdd:cd13995  148 DVYVPKDLRGTEIYMSPEVILCRGHNTKA-DIYSLGATIIHMQTGSPpwvrRYPRSAYPSYLYIIH-------------- 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 230 nknpvfagvrlpeiKEREPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHD 285
Cdd:cd13995  213 --------------KQAPPLEDIAQDCSPAMRELLEAALERNPNHRSSAAELLKHE 254
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
107-346 3.90e-14

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 74.91  E-value: 3.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 107 LF-QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAA--PGEVYTDYVATRWYRAPELLvGDVKYGKAV 183
Cdd:PTZ00283 148 LFiQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAAtvSDDVGRTFCGTPYYVAPEIW-RRKPYSKKA 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 184 DVWAIGCLVTEMFMGEPLFPGDsDIDQLYHimmclGNLIPRHQELfnknPvfagvrlPEIKereplerryPKLSEVVIDL 263
Cdd:PTZ00283 227 DMFSLGVLLYELLTLKRPFDGE-NMEEVMH-----KTLAGRYDPL----P-------PSIS---------PEMQEIVTAL 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 264 akkcLHIDPDKRPFCAELLHHDFFQ--MDGFAE------RFSQELQLKVQKDARNVSLSKKSQNRKKEKEKDDSLVEERK 335
Cdd:PTZ00283 281 ----LSSDPKRRPSSSKLLNMPICKlfISGLLEivqtqpGFSGPLRDTISRQIQQTKQLLQVERRRIVRQMEESLSTAAS 356
                        250
                 ....*....|.
gi 578809600 336 TLVVQdtNADP 346
Cdd:PTZ00283 357 TTILE--GATP 365
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
10-204 4.14e-14

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 72.80  E-value: 4.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMV-MKCRNKDTGriVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDHTIL 88
Cdd:cd05069   20 LGQGCFGEVwMGTWNGTTK--VAIKTL---KPGTMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEP-IYIVTEFMGKGSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRW 166
Cdd:cd05069   94 LDFLKEGDGKYLKLPQlvDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIE--DNEYTARQGAKF 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 167 ---YRAPELLVgdvkYGKAV---DVWAIGCLVTEMFM-GEPLFPG 204
Cdd:cd05069  172 pikWTAPEAAL----YGRFTiksDVWSFGILLTELVTkGRVPYPG 212
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
10-204 4.22e-14

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 72.80  E-value: 4.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRiVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDHTILD 89
Cdd:cd05071   17 LGQGCFGEVWMGTWNGTTR-VAIKTL---KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEP-IYIVTEYMSKGSLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  90 DLELFPNGLDYQVVQKYLF--QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTDYVATRW- 166
Cdd:cd05071   92 DFLKGEMGKYLRLPQLVDMaaQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIE--DNEYTARQGAKFp 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 578809600 167 --YRAPELLVgdvkYGKAV---DVWAIGCLVTEMFM-GEPLFPG 204
Cdd:cd05071  170 ikWTAPEAAL----YGRFTiksDVWSFGILLTELTTkGRVPYPG 209
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
2-191 6.13e-14

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 73.88  E-value: 6.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYENLGLVGEGSYGMVMKCRNKD--TGRIVAIKKFLESDDDKMVKKIAM----REIKLLKQL-RHENLVNLLEVCKKKK 74
Cdd:COG5752   32 ERYRAIKPLGQGGFGRTFLAVDEDipSHPHCVIKQFYFPEQGPSSFQKAVelfrQEAVRLDELgKHPQIPELLAYFEQDQ 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  75 RWYLVFEFVD-HTILDDLE---LFPNGLDYQVVQKYL--FQIIngigfcHSHNIIHRDIKPENILVSQS-GVVKLCDFGF 147
Cdd:COG5752  112 RLYLVQEFIEgQTLAQELEkkgVFSESQIWQLLKDLLpvLQFI------HSRNVIHRDIKPANIIRRRSdGKLVLIDFGV 185
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 148 AR-----TLAAPGEVytdyVATRWYRAPELLVGDVKYgkAVDVWAIG--CL 191
Cdd:COG5752  186 AKlltitALLQTGTI----IGTPEYMAPEQLRGKVFP--ASDLYSLGvtCI 230
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
10-276 6.91e-14

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 71.75  E-value: 6.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDdKMVKKIAMrEIKLLKQL-RHENLVNLLEvckkkkrwylvfEFVDHT-- 86
Cdd:cd13975    8 LGRGQYGVVYACDSWGGHFPCALKSVVPPDD-KHWNDLAL-EFHYTRSLpKHERIVSLHG------------SVIDYSyg 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ---------ILDDL--ELFPN---GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA 152
Cdd:cd13975   74 ggssiavllIMERLhrDLYTGikaGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 153 A-PGEVytdyVATRWYRAPELLVGdvKYGKAVDVWAIGCLvtemfmgeplfpgdsdidqLYHImmCLGNL-IPRHQELF- 229
Cdd:cd13975  154 MmSGSI----VGTPIHMAPELFSG--KYDNSVDVYAFGIL-------------------FWYL--CAGHVkLPEAFEQCa 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 578809600 230 NKNPVFAGVRlpeiKEREPleRRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd13975  207 SKDHLWNNVR----KGVRP--ERLPVFDEECWNLMEACWSGDPSQRP 247
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
11-204 7.15e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 71.53  E-value: 7.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKFLESDddkmvkkiamREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDD 90
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIE----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  91 lelFPNG-----LDYQVVQKYLFQIINGIGFCHSH---NIIHRDIKPENILVSQSGVVKLCDFGFARTLAApgEVYTDYV 162
Cdd:cd14060   72 ---YLNSneseeMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSH--TTHMSLV 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809600 163 ATRWYRAPELLVGdVKYGKAVDVWAIGCLVTEMFMGEPLFPG 204
Cdd:cd14060  147 GTFPWMAPEVIQS-LPVSETCDTYSYGVVLWEMLTREVPFKG 187
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
10-281 9.87e-14

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 71.92  E-value: 9.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKD-TGR----IVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05045    8 LGEGEFGKVVKATAFRlKGRagytTVAVKMLKENASSSELRDL-LSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTIL---------------------DDLELFPNG---LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVV 140
Cdd:cd05045   87 YGSLrsflresrkvgpsylgsdgnrNSSYLDNPDeraLTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVAEGRKM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 141 KLCDFGFARtlaapgEVYTD---------YVATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGdsdidq 210
Cdd:cd05045  167 KISDFGLSR------DVYEEdsyvkrskgRIPVKWM-AIESLFDHI-YTTQSDVWSFGVLLWEIVtLGGNPYPG------ 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 211 lyhimmclgnlIPRhQELFNKnpVFAGVRLpeikerepleRRYPKLSEVVIDLAKKCLHIDPDKRPFCAEL 281
Cdd:cd05045  233 -----------IAP-ERLFNL--LKTGYRM----------ERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
9-199 1.26e-13

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 70.79  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKF-LESDDDKMVKKIAMR-EIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd14148    1 IIGVGGFGKVYKGLWR--GEEVAVKAArQDPDEDIAVTAENVRqEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSHN---IIHRDIKPENILVSQ--------SGVVKLCDFGFAR------ 149
Cdd:cd14148   79 ALNRA-LAGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILEpienddlsGKTLKITDFGLARewhktt 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 578809600 150 TLAAPGevytdyvaTRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGE 199
Cdd:cd14148  158 KMSAAG--------TYAWMAPEVIRLSL-FSKSSDVWSFGVLLWELLTGE 198
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
10-195 1.44e-13

Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 70.58  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIK-KFLESDDDKMvkkiaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKmNTLSSNRANM-----LREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILV-----SQSGVVKlcDFGFARTL--AAPGEVYTDY 161
Cdd:cd14155   76 EQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdenGYTAVVG--DFGLAEKIpdYSDGKEKLAV 153
                        170       180       190
                 ....*....|....*....|....*....|....
gi 578809600 162 VATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEM 195
Cdd:cd14155  154 VGSPYWMAPEVLRGEP-YNEKADVFSYGIILCEI 186
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
22-288 1.52e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 72.74  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  22 RNKDTGRIVAIK----------KFLESDDDKMVKkIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF-----VDHT 86
Cdd:PTZ00267  77 RNPTTAAFVATRgsdpkekvvaKFVMLNDERQAA-YARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYgsggdLNKQ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ILDDLELFPNGLDYQVVQKYlFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR--TLAAPGEVYTDYVAT 164
Cdd:PTZ00267 156 IKQRLKEHLPFQEYEVGLLF-YQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKqySDSVSLDVASSFCGT 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 165 RWYRAPELLVGDvKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDqlyhIMmclgnliprHQELFNK-NPVFAGVRLPEI 243
Cdd:PTZ00267 235 PYYLAPELWERK-RYSKKADMWSLGVILYELLTLHRPFKGPSQRE----IM---------QQVLYGKyDPFPCPVSSGMK 300
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 244 KEREPLerrypklsevvidLAKkclhiDPDKRPFCAELLHHDFFQ 288
Cdd:PTZ00267 301 ALLDPL-------------LSK-----NPALRPTTQQLLHTEFLK 327
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
13-288 1.82e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 72.62  E-value: 1.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  13 GSYGMVMKCRNKDTGRIVAIKKFLESDddkmvkkiAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLE 92
Cdd:PHA03211 180 GSEGCVFESSHPDYPQRVVVKAGWYAS--------SVHEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRSDLYTYLG 251
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  93 LFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG---FAR-TLAAPgeVYTDYVATRWYR 168
Cdd:PHA03211 252 ARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGaacFARgSWSTP--FHYGIAGTVDTN 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 169 APELLVGDvKYGKAVDVWAIGCLVTEMFM-GEPLF---------PGDSDIDQlyhimmclgnLIPRHQELFNKNPVFAGV 238
Cdd:PHA03211 330 APEVLAGD-PYTPSVDIWSAGLVIFEAAVhTASLFsasrgderrPYDAQILR----------IIRQAQVHVDEFPQHAGS 398
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 239 RL-PEIKER----------EPLERRYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:PHA03211 399 RLvSQYRHRaarnrrpaytRPAWTRYYKLDLDVEYLVCRALTFDGARRPSAAELLRLPLFQ 459
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
10-290 1.90e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 70.91  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAikkFLESDDDKMVKKIAMR---EIKLLKQLRHENLVNLLE----VCKKKKRWYLVFEF 82
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVA---WCELQDRKLTKAEQQRfkeEAEMLKGLQHPNIVRFYDswesVLKGKKCIVLVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVS-QSGVVKLCDFGFARTLAApgEVYT 159
Cdd:cd14031   95 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLMRT--SFAK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLvgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMclGNLIPRHqelFNKnpvfagVR 239
Cdd:cd14031  173 SVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVT--SGIKPAS---FNK------VT 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 240 LPEIKEreplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDFFQMD 290
Cdd:cd14031  240 DPEVKE-----------------IIEGCIRQNKSERLSIKDLLNHAFFAED 273
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
10-288 1.91e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 70.85  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAikkFLESDDDKMVKKIAMR---EIKLLKQLRHENLVNLLE----VCKKKKRWYLVFEF 82
Cdd:cd14030   33 IGRGSFKTVYKGLDTETTVEVA---WCELQDRKLSKSERQRfkeEAGMLKGLQHPNIVRFYDswesTVKGKKCIVLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVS-QSGVVKLCDFGFARTLAApgEVYT 159
Cdd:cd14030  110 MTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRA--SFAK 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DYVATRWYRAPELLvgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYhimmclgnlipRHQELFNKNPVFAGVR 239
Cdd:cd14030  188 SVIGTPEFMAPEMY--EEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIY-----------RRVTSGVKPASFDKVA 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 578809600 240 LPEIKEreplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd14030  255 IPEVKE-----------------IIEGCIRQNKDERYAIKDLLNHAFFQ 286
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
6-196 2.00e-13

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 70.36  E-value: 2.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   6 NLGLVGEGSYGMvmKCRNKDtgriVAIKkFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDH 85
Cdd:cd05115   16 NFGCVKKGVYKM--RKKQID----VAIK-VLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMASG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDlelFPNGLDYQV----VQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDY 161
Cdd:cd05115   88 GPLNK---FLSGKKDEItvsnVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSYYKAR 164
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 578809600 162 VATRW---YRAPELLVGDvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05115  165 SAGKWplkWYAPECINFR-KFSSRSDVWSYGVTMWEAF 201
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
9-199 2.19e-13

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 70.28  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGR---IVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05065   11 VIGAGEFGEVCRGRLKLPGKreiFVAIKTLKSGYTEKQRRDF-LSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLeLFPNGLDYQVVQ--KYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA--APGEVYTDY 161
Cdd:cd05065   90 GALDSF-LRQNDGQFTVIQlvGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEddTSDPTYTSS 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809600 162 ----VATRWyRAPElLVGDVKYGKAVDVWAIGCLVTE-MFMGE 199
Cdd:cd05065  169 lggkIPIRW-TAPE-AIAYRKFTSASDVWSYGIVMWEvMSYGE 209
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
3-196 2.38e-13

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 70.63  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCR-------NKDTgrIVAIKKFLESDDDKMvKKIAMREIKLLKQLRHENLVNLLEVCKKKKR 75
Cdd:cd05050    6 NIEYVRDIGQGAFGRVFQARapgllpyEPFT--MVAVKMLKEEASADM-QADFQREAALMAEFDHPNIVKLLGVCAVGKP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  76 WYLVFEFVDHTIL-----------------DDLELFPNGLDY-----QVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL 133
Cdd:cd05050   83 MCLLFEYMAYGDLneflrhrspraqcslshSTSSARKCGLNPlplscTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 134 VSQSGVVKLCDFGFARTLAApGEVY----TDYVATRWYrAPELLVGDvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05050  163 VGENMVVKIADFGLSRNIYS-ADYYkaseNDAIPIRWM-PPESIFYN-RYTTESDVWAYGVVLWEIF 226
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
27-276 2.86e-13

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 70.11  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  27 GRIVAIKKFLESDDDKmvkKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDLELFPN-GLDYQVVQK 105
Cdd:cd13992   25 GRTVAIKHITFSRTEK---RTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREiKMDWMFKSS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 106 YLFQIINGIGFCHSHNII-HRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTDYVATR---WYRAPELLVGDvkygk 181
Cdd:cd13992  102 FIKDIVKGMNYLHSSSIGyHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHkklLWTAPELLRGS----- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 182 avdvwaigclvtemfMGEPLFPGDSDIdqlYHIMMCLgnliprhQELFNKNPVFAGVRLPEIKEREPLERRYPKLSEV-- 259
Cdd:cd13992  177 ---------------LLEVRGTQKGDV---YSFAIIL-------YEILFRSDPFALEREVAIVEKVISGGNKPFRPELav 231
                        250       260
                 ....*....|....*....|....*
gi 578809600 260 --------VIDLAKKCLHIDPDKRP 276
Cdd:cd13992  232 lldefpprLVLLVKQCWAENPEKRP 256
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
2-231 2.89e-13

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 71.41  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   2 EKYE----NLGL---VGEGSYGMVMKCR-----NKDTGRIVAIKkFLESDDDKMVKKIAMREIKLLKQL-RHENLVNLLE 68
Cdd:cd05106   31 EKWEfprdNLQFgktLGAGAFGKVVEATafglgKEDNVLRVAVK-MLKASAHTDEREALMSELKILSHLgQHKNIVNLLG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  69 VC----------------------KKKKRWYLVFEFVDHTILDDLELFPN------------GLDYQVVQKYL------- 107
Cdd:cd05106  110 ACthggpvlviteyccygdllnflRKKAETFLNFVMALPEISETSSDYKNitlekkyirsdsGFSSQGSDTYVemrpvss 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 108 -----------------------------FQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgevy 158
Cdd:cd05106  190 sssqssdskdeedtedswpldlddllrfsSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMND---- 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TDYVA-------TRWYrAPELLVgDVKYGKAVDVWAIGCLVTEMF-MGEPLFPG--------------------DSDIDQ 210
Cdd:cd05106  266 SNYVVkgnarlpVKWM-APESIF-DCVYTVQSDVWSYGILLWEIFsLGKSPYPGilvnskfykmvkrgyqmsrpDFAPPE 343
                        330       340
                 ....*....|....*....|.
gi 578809600 211 LYHIMMCLGNLIPRHQELFNK 231
Cdd:cd05106  344 IYSIMKMCWNLEPTERPTFSQ 364
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
9-282 3.04e-13

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 70.41  E-value: 3.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTG-----RIVAIKKFLESDDDKMVKKiamrEIKLLKQL-RHENLVNLLEVCKKKKRWYLVFEF 82
Cdd:cd05088   14 VIGEGNFGQVLKARIKKDGlrmdaAIKRMKEYASKDDHRDFAG----ELEVLCKLgHHPNIINLLGACEHRGYLYLAIEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDD-------LELFP---------NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd05088   90 APHGNLLDflrksrvLETDPafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTLAAPGEVYTDYVATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEM--FMGEPlfpgdsdidqlYHIMMClgnlipr 224
Cdd:cd05088  170 LSRGQEVYVKKTMGRLPVRWM-AIESLNYSV-YTTNSDVWSYGVLLWEIvsLGGTP-----------YCGMTC------- 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 225 hQELFNKNPVfaGVRLpeikeREPLerrypKLSEVVIDLAKKCLHIDPDKRPFCAELL 282
Cdd:cd05088  230 -AELYEKLPQ--GYRL-----EKPL-----NCDDEVYDLMRQCWREKPYERPSFAQIL 274
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
9-202 5.19e-13

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 69.39  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesddDKmvKKIAMR--EIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHT 86
Cdd:cd05606    1 IIGRGGFGEVYGCRKADTGKMYAMKCL-----DK--KRIKMKqgETLALNERIMLSLVSTGGDCPFIVCMTYAFQTPDKL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 --ILDDLelfpNG--LDYQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArtla 152
Cdd:cd05606   74 cfILDLM----NGgdLHYHLSQHGVFseaemrfyaaEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA---- 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 153 apgevyTDY--------VATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05606  146 ------CDFskkkphasVGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPF 197
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
9-217 5.39e-13

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 69.30  E-value: 5.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKcrnkdtGRI---VAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEF--- 82
Cdd:cd14063    7 VIGKGRFGRVHR------GRWhgdVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLckg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 --VDHTILDDLELFPNGLDYQVVQkylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVkLCDFGF---ARTLAAPGEV 157
Cdd:cd14063   81 rtLYSLIHERKEKFDFNKTVQIAQ----QICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLfslSGLLQPGRRE 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 158 YTDYVATRW--YRAPELL---------VGDVKYGKAVDVWAIGCLVTEMFMGEplFP-GDSDIDQLYHIMMC 217
Cdd:cd14063  156 DTLVIPNGWlcYLAPEIIralspdldfEESLPFTKASDVYAFGTVWYELLAGR--WPfKEQPAESIIWQVGC 225
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
10-211 6.20e-13

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 68.96  E-value: 6.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTgriVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKkRWYLVFEFVDHTIL- 88
Cdd:cd14062    1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKP-QLAIVTQWCEGSSLy 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtlaapgevytdyVATRW-- 166
Cdd:cd14062   77 KHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAT------------VKTRWsg 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 167 ------------YRAPEL--LVGDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQL 211
Cdd:cd14062  145 sqqfeqptgsilWMAPEVirMQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQI 203
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
10-290 6.86e-13

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 68.95  E-value: 6.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEV----CKKKKRWYLVFEFVDH 85
Cdd:cd14032    9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFwescAKGKRCIVLVTELMTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHN--IIHRDIKPENILVS-QSGVVKLCDFGFARTLAApgEVYTDYV 162
Cdd:cd14032   89 GTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATLKRA--SFAKSVI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 ATRWYRAPELLvgDVKYGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIMMClgnliprhqelFNKNPVFAGVRLPE 242
Cdd:cd14032  167 GTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTC-----------GIKPASFEKVTDPE 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 578809600 243 IKEreplerrypklsevvidLAKKCLHIDPDKRPFCAELLHHDFFQMD 290
Cdd:cd14032  234 IKE-----------------IIGECICKNKEERYEIKDLLSHAFFAED 264
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
98-261 8.02e-13

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 70.04  E-value: 8.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  98 LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD---YVATRWYrAPELLV 174
Cdd:cd05107  236 LSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKgstFLPLKWM-APESIF 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 175 GDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGDSDIDQLYhimmclgNLIPRHQELfnKNPVFAGVRLPEIKER---EPLE 250
Cdd:cd05107  315 NNL-YTTLSDVWSFGILLWEIFtLGGTPYPELPMNEQFY-------NAIKRGYRM--AKPAHASDEIYEIMQKcweEKFE 384
                        170
                 ....*....|.
gi 578809600 251 RRyPKLSEVVI 261
Cdd:cd05107  385 IR-PDFSQLVH 394
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
9-199 8.19e-13

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 68.74  E-value: 8.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGR---IVAIKKFLESDDDKMvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDH 85
Cdd:cd05066   11 VIGAGEFGEVCSGRLKLPGKreiPVAIKTLKAGYTEKQ-RRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMEN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  86 TILDDLeLFPNGLDYQVVQkyLFQIINGIG----FCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA-APGEVYTD 160
Cdd:cd05066   90 GSLDAF-LRKHDGQFTVIQ--LVGMLRGIAsgmkYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEdDPEAAYTT 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 578809600 161 Y---VATRWyRAPElLVGDVKYGKAVDVWAIGCLVTE-MFMGE 199
Cdd:cd05066  167 RggkIPIRW-TAPE-AIAYRKFTSASDVWSYGIVMWEvMSYGE 207
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
10-196 1.17e-12

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 68.53  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVM--KCRN--KDTGRI-VAIKKFLESDDDKmvKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05093   13 LGEGAFGKVFlaECYNlcPEQDKIlVAVKTLKDASDNA--RKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTILD--------DLELFPNGLD-YQVVQKYLF----QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtl 151
Cdd:cd05093   91 HGDLNkflrahgpDAVLMAEGNRpAELTQSQMLhiaqQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSR-- 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 152 aapgEVY-TDY--------VATRWYrAPELLVGDvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05093  169 ----DVYsTDYyrvgghtmLPIRWM-PPESIMYR-KFTTESDVWSLGVVLWEIF 216
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
9-202 1.52e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 68.54  E-value: 1.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKFlesddDKmvKKIAMREIKLLKqLRHENLVNLleVCKKKKRWYLVFEFVDHT-- 86
Cdd:cd14223    7 IIGRGGFGEVYGCRKADTGKMYAMKCL-----DK--KRIKMKQGETLA-LNERIMLSL--VSTGDCPFIVCMSYAFHTpd 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  87 ----ILDDLelfpNG--LDYQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART 150
Cdd:cd14223   77 klsfILDLM----NGgdLHYHLSQHGVFseaemrfyaaEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 578809600 151 LAAPGEVYTdyVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd14223  153 FSKKKPHAS--VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPF 202
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
9-276 1.70e-12

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 67.90  E-value: 1.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKDTGRIVAIKKF-LESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRwyLVFEFVDHTI 87
Cdd:cd14025    3 KVGSGGFGQVYKVRHKHWKTWLAIKCPpSLHVDDSERMEL-LEEAKKMEMAKFRHILPVYGICSEPVG--LVMEYMETGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDL---ELFPNGLDYQVVqkylFQIINGIGFCHSHN--IIHRDIKPENILVSQSGVVKLCDFGFAR--TLAAPGEVYTD 160
Cdd:cd14025   80 LEKLlasEPLPWELRFRII----HETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwnGLSHSHDLSRD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 161 -YVATRWYRAPELLVGDVK-YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIdqlYHIMMclgnliprhqelfnknPVFAGV 238
Cdd:cd14025  156 gLRGTIAYLPPERFKEKNRcPDTKHDVYSFAIVIWGILTQKKPFAGENNI---LHIMV----------------KVVKGH 216
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 578809600 239 RlPEIkerEPLERRYPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd14025  217 R-PSL---SPIPRQRPSECQQMICLMKRCWDQDPRKRP 250
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
3-276 2.01e-12

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 68.10  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLglVGEGSYGMVMKCRNKDTGR-----IVAIKKFLESDDDKMVKKiamrEIKLLKQL-RHENLVNLLEVCKKKKRW 76
Cdd:cd05089    5 KFEDV--IGEGNFGQVIKAMIKKDGLkmnaaIKMLKEFASENDHRDFAG----ELEVLCKLgHHPNIINLLGACENRGYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHTILDD-------LELFP---------NGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVV 140
Cdd:cd05089   79 YIAIEYAPYGNLLDflrksrvLETDPafakehgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 141 KLCDFGFARTlaapGEVYTD----YVATRWYrAPELLVGDVkYGKAVDVWAIGCLVTEM--FMGEPlfpgdsdidqlYHI 214
Cdd:cd05089  159 KIADFGLSRG----EEVYVKktmgRLPVRWM-AIESLNYSV-YTTKSDVWSFGVLLWEIvsLGGTP-----------YCG 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578809600 215 MMClgnliprhQELFNKNPvfAGVRLPEIKereplerrypKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd05089  222 MTC--------AELYEKLP--QGYRMEKPR----------NCDDEVYELMRQCWRDRPYERP 263
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
3-284 2.80e-12

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 68.13  E-value: 2.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESdddKMVKKIAMREIKLLKQLRHENL------------------- 63
Cdd:cd14217   13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSA---QHYTETALDEIKLLRCVRESDPedpnkdmvvqliddfkisg 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  64 VNLLEVCkkkkrwyLVFEFVDHTILD-DLELFPNGLDYQVVQKYLFQIINGIGFCHSH-NIIHRDIKPENILV------- 134
Cdd:cd14217   90 MNGIHVC-------MVFEVLGHHLLKwIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvddayv 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 135 ------------------SQSGV--------------------VKLCDFGFARTLAapgEVYTDYVATRWYRAPELLVGd 176
Cdd:cd14217  163 rrmaaeatewqkagapppSGSAVstapdllvnpldprnadkirVKIADLGNACWVH---KHFTEDIQTRQYRSIEVLIG- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 177 VKYGKAVDVWAIGCLVTEMFMGEPLFPGDS------DIDQLYHIMMCLGNlIPRH--------QELFNKNPvfagvRLPE 242
Cdd:cd14217  239 AGYSTPADIWSTACMAFELATGDYLFEPHSgedysrDEDHIAHIIELLGC-IPRHfalsgkysREFFNRRG-----ELRH 312
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 243 IKEREP------LERRYPKLSEVV---IDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14217  313 ITKLKPwslfdvLVEKYGWPHEDAaqfTDFLIPMLEMVPEKRASAGECLRH 363
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
22-288 4.42e-12

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 67.20  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  22 RNKDTGRIVAIKKF-LESDDDKMVKkIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTILDDL--ELFPNGL 98
Cdd:cd08226   20 RHTPTGTLVTVKITnLDNCSEEHLK-ALQNEVVLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSARGLlkTYFPEGM 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  99 DYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE---VYTDY----VATRWYRAPE 171
Cdd:cd08226   99 NEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGDGLVSLSGLSHLYSMVTNGQrskVVYDFpqfsTSVLPWLSPE 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 172 LLVGDVK-YGKAVDVWAIGCLVTEMFMGEPLFPGDSDIDQLYHIM-----MCLGNLIPRHQELFNKNP---VFAGV---- 238
Cdd:cd08226  179 LLRQDLHgYNVKSDIYSVGITACELARGQVPFQDMRRTQMLLQKLkgppySPLDIFPFPELESRMKNSqsgMDSGIgesv 258
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578809600 239 ---RLPEIKEREPLERRYPK-LSEVVIDLAKKCLHIDPDKRPFCAELLHHDFFQ 288
Cdd:cd08226  259 atsSMTRTMTSERLQTPSSKtFSPAFHNLVELCLQQDPEKRPSASSLLSHSFFK 312
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
10-202 4.50e-12

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 67.73  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRIVAIKKFLESD---DDKMVKKIAMREIklLKQLRHENLVNLLEVCKKKKRWYLVFEFVD-- 84
Cdd:cd05626    9 LGIGAFGEVCLACKVDTHALYAMKTLRKKDvlnRNQVAHVKAERDI--LAEADNEWVVKLYYSFQDKDNLYFVMDYIPgg 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 --HTILDDLELFPNGLdyqvVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTL----------- 151
Cdd:cd05626   87 dmMSLLIRMEVFPEVL----ARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthnskyyqk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 152 --------AAPGEVYTD----------------------------YVATRWYRAPELLVGDvKYGKAVDVWAIGCLVTEM 195
Cdd:cd05626  163 gshirqdsMEPSDLWDDvsncrcgdrlktleqratkqhqrclahsLVGTPNYIAPEVLLRK-GYTQLCDWWSVGVILFEM 241

                 ....*..
gi 578809600 196 FMGEPLF 202
Cdd:cd05626  242 LVGQPPF 248
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
3-332 5.85e-12

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 66.58  E-value: 5.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMK-CRNKDTGRI---VAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCkkkkrwyl 78
Cdd:cd05108    8 EFKKIKVLGSGAFGTVYKgLWIPEGEKVkipVAIKELREATSPKANKEI-LDEAYVMASVDNPHVCRLLGIC-------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  79 vfefVDHTILDDLELFPNG--LDY------QVVQKYLF----QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd05108   79 ----LTSTVQLITQLMPFGclLDYvrehkdNIGSQYLLnwcvQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 147 FARTLAAPGEVYT---DYVATRWYRAPELLvgDVKYGKAVDVWAIGCLVTE-MFMGEPLFPGdsdidqlyhimmclgnlI 222
Cdd:cd05108  155 LAKLLGAEEKEYHaegGKVPIKWMALESIL--HRIYTHQSDVWSYGVTVWElMTFGSKPYDG-----------------I 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 223 PRHQElfnKNPVFAGVRLPEikereplerryPKLSEV-VIDLAKKCLHIDPDKRPFCAELLhHDFFQMDGFAERFsqelq 301
Cdd:cd05108  216 PASEI---SSILEKGERLPQ-----------PPICTIdVYMIMVKCWMIDADSRPKFRELI-IEFSKMARDPQRY----- 275
                        330       340       350
                 ....*....|....*....|....*....|....
gi 578809600 302 LKVQKDARNVSLSKKSQNRK---KEKEKDDSLVE 332
Cdd:cd05108  276 LVIQGDERMHLPSPTDSNFYralMDEEDMDDVVD 309
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
83-276 6.78e-12

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 67.24  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLELfpnGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPgevyTDYV 162
Cdd:cd05104  199 VTSEILEEDEL---ALDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRND----SNYV 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 163 A-------TRWYrAPELLVGDVkYGKAVDVWAIGCLVTEMF-MGEPLFPGdSDIDQLYHIMmclgnliprhqelfnknpV 234
Cdd:cd05104  272 VkgnarlpVKWM-APESIFECV-YTFESDVWSYGILLWEIFsLGSSPYPG-MPVDSKFYKM------------------I 330
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 578809600 235 FAGVRLpEIKEREPLErrypklsevVIDLAKKCLHIDPDKRP 276
Cdd:cd05104  331 KEGYRM-DSPEFAPSE---------MYDIMRSCWDADPLKRP 362
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
11-146 7.75e-12

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 62.84  E-value: 7.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  11 GEGSYGMVMKCRNKDTGRIVAIKKFleSDDDKMVKKIAMREIKLLKQLR-HE-NLVNLLEVCKKKKRWYLVFEFVDHTIL 88
Cdd:cd13968    2 GEGASAKVFWAEGECTTIGVAVKIG--DDVNNEEGEDLESEMDILRRLKgLElNIPKVLVTEDVDGPNILLMELVKGGTL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600  89 DDLELFPNgLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd13968   80 IAYTQEEE-LDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
9-276 8.89e-12

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 65.71  E-value: 8.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNK---DTGRIVAIKK-----FLESDDDKMvkkiaMREIKLLKQLRHENLVNLLEVC---KKKKRW- 76
Cdd:cd05074   16 MLGKGEFGSVREAQLKsedGSFQKVAVKMlkadiFSSSDIEEF-----LREAACMKEFDHPNVIKLIGVSlrsRAKGRLp 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 --YLVFEFVDHtilDDLELF---------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDF 145
Cdd:cd05074   91 ipMVILPFMKH---GDLHTFllmsrigeePFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 146 GFARTLAApGEVYTDYVAT----RWYrAPELLVGDVkYGKAVDVWAIGCLVTE-MFMGEPLFPGDSDidqlyhimmclgn 220
Cdd:cd05074  168 GLSKKIYS-GDYYRQGCASklpvKWL-ALESLADNV-YTTHSDVWAFGVTMWEiMTRGQTPYAGVEN------------- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 221 liprhQELFNKnpVFAGVRLpeikeREPlerryPKLSEVVIDLAKKCLHIDPDKRP 276
Cdd:cd05074  232 -----SEIYNY--LIKGNRL-----KQP-----PDCLEDVYELMCQCWSPEPKCRP 270
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
10-196 1.51e-11

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 65.03  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR----NKDTGRIVAIKKFLESDDDKMVKKIaMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD- 84
Cdd:cd05090   13 LGECAFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQWNEF-QQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNq 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 ---HTIL-------------DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd05090   92 gdlHEFLimrsphsdvgcssDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLS 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 149 RtlaapgEVYT-DY--------VATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05090  172 R------EIYSsDYyrvqnkslLPIRWMPPEAIMYG--KFSSDSDIWSFGVVLWEIF 220
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1-202 1.54e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 65.85  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   1 MEKYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFlesddDKmvKKIAMREIKLLKqLRHENLVNLleVCKKKKRWYLVF 80
Cdd:cd05633    4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCL-----DK--KRIKMKQGETLA-LNERIMLSL--VSTGDCPFIVCM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  81 EFVDHT---ILDDLELFPNG-LDYQVVQKYLF----------QIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFG 146
Cdd:cd05633   74 TYAFHTpdkLCFILDLMNGGdLHYHLSQHGVFsekemrfyatEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLG 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 147 FARTLAAPGEVYTdyVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLF 202
Cdd:cd05633  154 LACDFSKKKPHAS--VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPF 207
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
3-284 1.57e-11

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 65.04  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   3 KYENLGLVGEGSYGMVMKCRNKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQL-RHENLVnllevckkkkRWYLVFE 81
Cdd:cd14138    6 EFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVV----------RYYSAWA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLelFPNG--------LDYQVVQKY--------LFQIINGIGFCHSHNIIHRDIKPENILVSQSG------- 138
Cdd:cd14138   76 EDDHMLIQNE--YCNGgsladaisENYRIMSYFtepelkdlLLQVARGLKYIHSMSLVHMDIKPSNIFISRTSipnaase 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 139 ------------VVKLCDFGFARTLAAPGEVYTDyvaTRwYRAPELLVGDVKYGKAVDVWAIGCLVTEMFMGEPLfPGDS 206
Cdd:cd14138  154 egdedewasnkvIFKIGDLGHVTRVSSPQVEEGD---SR-FLANEVLQENYTHLPKADIFALALTVVCAAGAEPL-PTNG 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 207 diDQLYHImmclgnlipRHQELfnknPvfagvRLPEIkereplerrypkLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14138  229 --DQWHEI---------RQGKL----P-----RIPQV------------LSQEFLDLLKVMIHPDPERRPSAVALVKH 274
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
10-204 1.62e-11

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 65.09  E-value: 1.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMV-MKCRNKDTGriVAIKKFlesDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKrWYLVFEFVDH-TI 87
Cdd:cd05070   17 LGNGQFGEVwMGTWNGNTK--VAIKTL---KPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEP-IYIVTEYMSKgSL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLE-------LFPNGLDYQVvqkylfQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAapGEVYTD 160
Cdd:cd05070   91 LDFLKdgegralKLPNLVDMAA------QVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIE--DNEYTA 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 578809600 161 YVATRW---YRAPELLVgdvkYGKAV---DVWAIGCLVTEMFM-GEPLFPG 204
Cdd:cd05070  163 RQGAKFpikWTAPEAAL----YGRFTiksDVWSFGILLTELVTkGRVPYPG 209
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
5-207 2.07e-11

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 64.72  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   5 ENLGLV---GEGSYGMV----MKCRNKDTGRI-VAIKKFLESDDDKMVKKIAMrEIKLLKQLRHENLVNLLEVCKKKKRW 76
Cdd:cd05036    6 KNLTLIralGQGAFGEVyegtVSGMPGDPSPLqVAVKTLPELCSEQDEMDFLM-EALIMSKFNHPNIVRCIGVCFQRLPR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  77 YLVFEFVDHtilDDLELF----------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSG---VVKLC 143
Cdd:cd05036   85 FILLELMAG---GDLKSFlrenrprpeqPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGpgrVAKIG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578809600 144 DFGFARtlaapgEVY-TDY--------VATRWYrAPELLVGDVKYGKaVDVWAIGCLVTEMF-MGEPLFPGDSD 207
Cdd:cd05036  162 DFGMAR------DIYrADYyrkggkamLPVKWM-PPEAFLDGIFTSK-TDVWSFGVLLWEIFsLGYMPYPGKSN 227
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
9-173 2.43e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 64.42  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVMKCRNKdtGRIVAIKKFLESDDdkmvkKIAMREIKLLKQ--LRHENLVNLLEV-CKKKKRW---YLVFEF 82
Cdd:cd14144    2 SVGKGRYGEVWKGKWR--GEKVAVKIFFTTEE-----ASWFRETEIYQTvlMRHENILGFIAAdIKGTGSWtqlYLITDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDHTILDDLeLFPNGLDYQVVQKYLFQIINGIGFCHSH--------NIIHRDIKPENILVSQSGVVKLCDFGFA-RTLAA 153
Cdd:cd14144   75 HENGSLYDF-LRGNTLDTQSMLKLAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLAvKFISE 153
                        170       180
                 ....*....|....*....|...
gi 578809600 154 PGEVY---TDYVATRWYRAPELL 173
Cdd:cd14144  154 TNEVDlppNTRVGTKRYMAPEVL 176
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
10-196 2.90e-11

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 64.26  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVM--KCRNKDTGR---IVAIKKFleSDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05094   13 LGEGAFGKVFlaECYNLSPTKdkmLVAVKTL--KDPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 H---------------TILDDLELFPNG-LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd05094   91 HgdlnkflrahgpdamILVDGQPRQAKGeLGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMS 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 149 RTLAApgevyTDY--------VATRWYrAPELLVGDvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05094  171 RDVYS-----TDYyrvgghtmLPIRWM-PPESIMYR-KFTTESDVWSFGVILWEIF 219
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
10-196 5.89e-11

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 63.50  E-value: 5.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTG-----RIVAIKKfLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVD 84
Cdd:cd05091   14 LGEDRFGKVYKGHLFGTApgeqtQAVAIKT-LKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSMIFSYCS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  85 HTIL----------------DDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFA 148
Cdd:cd05091   93 HGDLheflvmrsphsdvgstDDDKTVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKISDLGLF 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 578809600 149 RtlaapgEVYT-DY--------VATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEMF 196
Cdd:cd05091  173 R------EVYAaDYyklmgnslLPIRWMSPEAIMYG--KFSIDSDIWSYGVVLWEVF 221
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
7-284 6.59e-11

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 63.19  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMKCRNKDTGRIVAIKK----FLESDDDKMvkkiAMREIKLLKQL-RHENLVNLLEVCKKKKRWYLVFE 81
Cdd:cd14051    5 VEKIGSGEFGSVYKCINRLDGCVYAIKKskkpVAGSVDEQN----ALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVD----HTILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQS-GVVKLC--DFGFARTLAAP 154
Cdd:cd14051   81 YCNggslADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTpNPVSSEeeEEDFEGEEDNP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 155 GEVYTDYV------ATRwYRAPELLVGDVKY-------------GKAvDVWAIGCLVTEMFMGEPLfPGDSdiDQLYHIM 215
Cdd:cd14051  161 ESNEVTYKigdlghVTS-ISNPQVEEGDCRFlaneilqenyshlPKA-DIFALALTVYEAAGGGPL-PKNG--DEWHEIR 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578809600 216 MclGNLIPrhqelfnknpvfagvrlpeikereplerrYPKLSEVVIDLAKKCLHIDPDKRPFCAELLHH 284
Cdd:cd14051  236 Q--GNLPP-----------------------------LPQCSPEFNELLRSMIHPDPEKRPSAAALLQH 273
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
10-283 8.16e-11

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 62.61  E-value: 8.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCR-NKDTGRIVAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDhtiL 88
Cdd:cd05042    3 IGNGWFGKVLLGEiYSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCD---L 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  89 DDL----------ELFPNglDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 158
Cdd:cd05042   80 GDLkaylrserehERGDS--DTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYKEDYIE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 159 TD---YVATRWYrAPELL---------VGDVKYGkavDVWAIGCLVTEMF-MGEPLFPGDSDIDQLyhimmclgNLIPRH 225
Cdd:cd05042  158 TDdklWFPLRWT-APELVtefhdrllvVDQTKYS---NIWSLGVTLWELFeNGAQPYSNLSDLDVL--------AQVVRE 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 578809600 226 QElfnknpvfagVRLPEIKEREPLERRYpklsevvIDLAKKCLhIDPDKRPfCAELLH 283
Cdd:cd05042  226 QD----------TKLPKPQLELPYSDRW-------YEVLQFCW-LSPEQRP-AAEDVH 264
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
9-195 1.36e-10

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 62.29  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   9 LVGEGSYGMVmkCRNKDTGRiVAIKkFLESDDDKMVK-KIAMREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDHTI 87
Cdd:cd14152    7 LIGQGRWGKV--HRGRWHGE-VAIR-LLEIDGNNQDHlKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFCKGRT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  88 LDDLELFPN-GLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVsQSGVVKLCDFGFartLAAPGEVYTDY----- 161
Cdd:cd14152   83 LYSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGL---FGISGVVQEGRrenel 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 578809600 162 -VATRW--YRAPELL--------VGDVKYGKAVDVWAIGCLVTEM 195
Cdd:cd14152  159 kLPHDWlcYLAPEIVremtpgkdEDCLPFSKAADVYAFGTIWYEL 203
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
7-289 1.55e-10

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 61.90  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600   7 LGLVGEGSYGMVMK---CRNKDTGRI-VAIKKFLESDDDKMVKKIAMREIKLlKQLRHENLVNLLEVCKKKKrWYLVFEF 82
Cdd:cd05111   12 LKVLGSGVFGTVHKgiwIPEGDSIKIpVAIKVIQDRSGRQSFQAVTDHMLAI-GSLDHAYIVRLLGICPGAS-LQLVTQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  83 VDH-TILDDLELFPNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGE--VYT 159
Cdd:cd05111   90 LPLgSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLYPDDKkyFYS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 160 DY-VATRWYRAPELLVGdvKYGKAVDVWAIGCLVTEM--FMGEPlfpgdsdidqlyhimmclgnliprhqelfnknpvFA 236
Cdd:cd05111  170 EAkTPIKWMALESIHFG--KYTHQSDVWSYGVTVWEMmtFGAEP----------------------------------YA 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 578809600 237 GVRLPEIKEREPLERRYPKLSEVVIDLAK---KCLHIDPDKRPFCAELLhHDFFQM 289
Cdd:cd05111  214 GMRLAEVPDLLEKGERLAQPQICTIDVYMvmvKCWMIDENIRPTFKELA-NEFTRM 268
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
10-230 2.76e-10

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 61.18  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKCRNKDTGRI--VAIKKFLESDDDKMVKKIAMREIKLLKQLRHENLVNLLEVCKK--KKRWY----LVFE 81
Cdd:cd05075    8 LGEGEFGSVMEGQLNQDDSVlkVAVKTMKIAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQntESEGYpspvVILP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  82 FVDHTILDDLELF------PNGLDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApG 155
Cdd:cd05075   88 FMKHGDLHSFLLYsrlgdcPVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKKIYN-G 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 156 EVYTD----YVATRWYRAPELlvGDVKYGKAVDVWAIGCLVTEMFM-GEPLFPG--DSDI-----------------DQL 211
Cdd:cd05075  167 DYYRQgrisKMPVKWIAIESL--ADRVYTTKSDVWSFGVTMWEIATrGQTPYPGveNSEIydylrqgnrlkqppdclDGL 244
                        250
                 ....*....|....*....
gi 578809600 212 YHIMMCLGNLIPRHQELFN 230
Cdd:cd05075  245 YELMSSCWLLNPKDRPSFE 263
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
118-284 2.85e-10

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 61.27  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 118 HSHNIIHRDIKPENI-LVSQSGVVKLCDFGFARTLAAPGEVYTDYVATRWYRAPELLVGDVKYGKAVDVWAIGCLVTEMF 196
Cdd:cd13974  149 HKKNIVHRDLKLGNMvLNKRTRKITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYLGKPSDMWALGVVLFTML 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 197 MGEplFPG-DSdidqlyhimmclgnlIPrhQELFNKnpvfagvrlpeIKERE---PLERRypkLSEVVIDLAKKCLHIDP 272
Cdd:cd13974  229 YGQ--FPFyDS---------------IP--QELFRK-----------IKAAEytiPEDGR---VSENTVCLIRKLLVLNP 275
                        170
                 ....*....|..
gi 578809600 273 DKRPFCAELLHH 284
Cdd:cd13974  276 QKRLTASEVLDS 287
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
10-199 3.18e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 61.13  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  10 VGEGSYGMVMKcRNKDTGRIVAIKKF--------LESDDDKMVKKI----AMR-------EIKLLKQLRHENLVNLLEVC 70
Cdd:cd14067    1 LGQGGSGTVIY-RARYQGQPVAVKRFhikkckkrTDGSADTMLKHLraadAMKnfsefrqEASMLHSLQHPCIVYLIGIS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  71 KkkkrwylvfefvdHTILDDLELFPNG-----------------LDYQVVQKYLFQIINGIGFCHSHNIIHRDIKPENIL 133
Cdd:cd14067   80 I-------------HPLCFALELAPLGslntvleenhkgssfmpLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNIL 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578809600 134 VSQSGV-----VKLCDFGFARTLAAPGEVYTDyvATRWYRAPELLVGDVkYGKAVDVWAIGCLVTEMFMGE 199
Cdd:cd14067  147 VWSLDVqehinIKLSDYGISRQSFHEGALGVE--GTPGYQAPEIRPRIV-YDEKVDMFSYGMVLYELLSGQ 214
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
49-283 3.48e-10

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 60.77  E-value: 3.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600  49 MREIKLLKQLRHENLVNLLEVCKKKKRWYLVFEFVDhtiLDDLE-----------LFPNGLdyqVVQKYLFQIINGIGFC 117
Cdd:cd05087   45 LEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCP---LGDLKgylrscraaesMAPDPL---TLQRMACEVACGLLHL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 118 HSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD---YVATRWYrAPE--------LLVGDVKygKAVDVW 186
Cdd:cd05087  119 HRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYKEDYFVTAdqlWVPLRWI-APElvdevhgnLLVVDQT--KQSNVW 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578809600 187 AIGCLVTEMF-MGEPLFPGDSDIDQLYHIMmclgnlipRHQELfnknpvfagvRLPEIKEREPLERRYpklsevvIDLAK 265
Cdd:cd05087  196 SLGVTIWELFeLGNQPYRHYSDRQVLTYTV--------REQQL----------KLPKPQLKLSLAERW-------YEVMQ 250
                        250
                 ....*....|....*...
gi 578809600 266 KCLhIDPDKRPfCAELLH 283
Cdd:cd05087  251 FCW-LQPEQRP-TAEEVH 266
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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